Loading…
Eyes absent represents a class of protein tyrosine phosphatases
The Eyes absent proteins are members of a conserved regulatory network implicated in the development of the eye, muscle, kidney and ear 1 , 2 , 3 , 4 , 5 , 6 , 7 . Mutations in the Eyes absent genes have been associated with several congenital disorders including the multi-organ disease bronchio-oto...
Saved in:
| Published in: | Nature (London) 2003-11, Vol.426 (6964), p.295-298 |
|---|---|
| Main Authors: | , , , , , , |
| Format: | Article |
| Language: | English |
| Subjects: | |
| Citations: | Items that this one cites Items that cite this one |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| cited_by | cdi_FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3 |
|---|---|
| cites | cdi_FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3 |
| container_end_page | 298 |
| container_issue | 6964 |
| container_start_page | 295 |
| container_title | Nature (London) |
| container_volume | 426 |
| creator | Rayapureddi, Jayanagendra P. Kattamuri, Chandramohan Steinmetz, Brian D. Frankfort, Benjamin J. Ostrin, Edwin J. Mardon, Graeme Hegde, Rashmi S. |
| description | The Eyes absent proteins are members of a conserved regulatory network implicated in the development of the eye, muscle, kidney and ear
1
,
2
,
3
,
4
,
5
,
6
,
7
. Mutations in the Eyes absent genes have been associated with several congenital disorders including the multi-organ disease bronchio-oto-renal syndrome
8
, congenital cataracts
9
and late-onset deafness
10
. On the basis of previous analyses it has been shown that Eyes absent is a nuclear transcription factor, acting through interaction with homeodomain-containing Sine oculis (also known as Six) proteins
11
. Here we show that Eyes absent is also a protein tyrosine phosphatase. It does not resemble the classical tyrosine phosphatases that use cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate
12
. Rather, Eyes absent is the prototype for a class of protein tyrosine phosphatases that use a nucleophilic aspartic acid in a metal-dependent reaction. Furthermore, the phosphatase activity of Eyes absent contributes to its ability to induce eye formation in
Drosophila
. |
| doi_str_mv | 10.1038/nature02093 |
| format | article |
| fullrecord | <record><control><sourceid>gale_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_743579430</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A187810712</galeid><sourcerecordid>A187810712</sourcerecordid><originalsourceid>FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3</originalsourceid><addsrcrecordid>eNqF0t9r1DAcAPAiijunT75L2XAi2vlNkzbpkxzH1MFQ0ImPIc19c-vopV2SgvffL-UObidVSSAh-eSbX98keUngnAAVH6wKg0PIoaKPkhlhvMxYKfjjZAaQiwwELY-SZ97fAkBBOHuaHBFW5gKKfJZ8vNigT1Xt0YbUYe9w7MWRVLfK-7Qzae-6gI1Nw8Z1vrGY9jed729UUB798-SJUa3HF7v2OPn56eJ68SW7-vb5cjG_ynTJWMhqyDmW1GhaKiCGUYbIBDBNYjXx5HRp8qpYMqixQKM1GEOhMBViTpDX9Dh5s40bT3M3oA9y3XiNbassdoOXnNGCV4xClGf_loSKiufFfyERoiqYIBGe_AFvu8HZeF2ZAytIxVke0ekWrVSLsrGmC07pMaKcE8EFAU5GlU2oFVp0qu0smiYOH_iTCa_75k4-ROcTKJYlrhs9GfXtwYJoAv4OKzV4Ly9_fD-07_5u59e_Fl8ntY654h0a2btmrdxGEpBjtsoH2Rr1q93DDvUal3u7S88IXu-A8lq1ximrG793BaXxK8dA77fOxym7Qrf_oal97wE92vvJ</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>204519742</pqid></control><display><type>article</type><title>Eyes absent represents a class of protein tyrosine phosphatases</title><source>Nature</source><creator>Rayapureddi, Jayanagendra P. ; Kattamuri, Chandramohan ; Steinmetz, Brian D. ; Frankfort, Benjamin J. ; Ostrin, Edwin J. ; Mardon, Graeme ; Hegde, Rashmi S.</creator><creatorcontrib>Rayapureddi, Jayanagendra P. ; Kattamuri, Chandramohan ; Steinmetz, Brian D. ; Frankfort, Benjamin J. ; Ostrin, Edwin J. ; Mardon, Graeme ; Hegde, Rashmi S.</creatorcontrib><description>The Eyes absent proteins are members of a conserved regulatory network implicated in the development of the eye, muscle, kidney and ear
1
,
2
,
3
,
4
,
5
,
6
,
7
. Mutations in the Eyes absent genes have been associated with several congenital disorders including the multi-organ disease bronchio-oto-renal syndrome
8
, congenital cataracts
9
and late-onset deafness
10
. On the basis of previous analyses it has been shown that Eyes absent is a nuclear transcription factor, acting through interaction with homeodomain-containing Sine oculis (also known as Six) proteins
11
. Here we show that Eyes absent is also a protein tyrosine phosphatase. It does not resemble the classical tyrosine phosphatases that use cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate
12
. Rather, Eyes absent is the prototype for a class of protein tyrosine phosphatases that use a nucleophilic aspartic acid in a metal-dependent reaction. Furthermore, the phosphatase activity of Eyes absent contributes to its ability to induce eye formation in
Drosophila
.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/nature02093</identifier><identifier>PMID: 14628052</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; Animals ; Biological and medical sciences ; Cataracts ; Cell differentiation, maturation, development, hematopoiesis ; Cell physiology ; Drosophila melanogaster - embryology ; Drosophila melanogaster - enzymology ; Drosophila melanogaster - genetics ; Drosophila Proteins - antagonists & inhibitors ; Drosophila Proteins - chemistry ; Drosophila Proteins - metabolism ; Eye - embryology ; Eye - enzymology ; Eye - metabolism ; Eye Proteins - antagonists & inhibitors ; Eye Proteins - chemistry ; Eye Proteins - metabolism ; Eyes & eyesight ; Fundamental and applied biological sciences. Psychology ; Humanities and Social Sciences ; letter ; Molecular and cellular biology ; Molecular Sequence Data ; multidisciplinary ; Mutation ; Phosphorylation ; Protein Tyrosine Phosphatases - antagonists & inhibitors ; Protein Tyrosine Phosphatases - chemistry ; Protein Tyrosine Phosphatases - metabolism ; Proteins ; Science ; Science (multidisciplinary) ; Substrate Specificity</subject><ispartof>Nature (London), 2003-11, Vol.426 (6964), p.295-298</ispartof><rights>Macmillan Magazines Ltd. 2003</rights><rights>2004 INIST-CNRS</rights><rights>COPYRIGHT 2003 Nature Publishing Group</rights><rights>Copyright Macmillan Journals Ltd. Nov 20, 2003</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3</citedby><cites>FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15339723$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14628052$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rayapureddi, Jayanagendra P.</creatorcontrib><creatorcontrib>Kattamuri, Chandramohan</creatorcontrib><creatorcontrib>Steinmetz, Brian D.</creatorcontrib><creatorcontrib>Frankfort, Benjamin J.</creatorcontrib><creatorcontrib>Ostrin, Edwin J.</creatorcontrib><creatorcontrib>Mardon, Graeme</creatorcontrib><creatorcontrib>Hegde, Rashmi S.</creatorcontrib><title>Eyes absent represents a class of protein tyrosine phosphatases</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The Eyes absent proteins are members of a conserved regulatory network implicated in the development of the eye, muscle, kidney and ear
1
,
2
,
3
,
4
,
5
,
6
,
7
. Mutations in the Eyes absent genes have been associated with several congenital disorders including the multi-organ disease bronchio-oto-renal syndrome
8
, congenital cataracts
9
and late-onset deafness
10
. On the basis of previous analyses it has been shown that Eyes absent is a nuclear transcription factor, acting through interaction with homeodomain-containing Sine oculis (also known as Six) proteins
11
. Here we show that Eyes absent is also a protein tyrosine phosphatase. It does not resemble the classical tyrosine phosphatases that use cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate
12
. Rather, Eyes absent is the prototype for a class of protein tyrosine phosphatases that use a nucleophilic aspartic acid in a metal-dependent reaction. Furthermore, the phosphatase activity of Eyes absent contributes to its ability to induce eye formation in
Drosophila
.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cataracts</subject><subject>Cell differentiation, maturation, development, hematopoiesis</subject><subject>Cell physiology</subject><subject>Drosophila melanogaster - embryology</subject><subject>Drosophila melanogaster - enzymology</subject><subject>Drosophila melanogaster - genetics</subject><subject>Drosophila Proteins - antagonists & inhibitors</subject><subject>Drosophila Proteins - chemistry</subject><subject>Drosophila Proteins - metabolism</subject><subject>Eye - embryology</subject><subject>Eye - enzymology</subject><subject>Eye - metabolism</subject><subject>Eye Proteins - antagonists & inhibitors</subject><subject>Eye Proteins - chemistry</subject><subject>Eye Proteins - metabolism</subject><subject>Eyes & eyesight</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humanities and Social Sciences</subject><subject>letter</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Mutation</subject><subject>Phosphorylation</subject><subject>Protein Tyrosine Phosphatases - antagonists & inhibitors</subject><subject>Protein Tyrosine Phosphatases - chemistry</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Proteins</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Substrate Specificity</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNqF0t9r1DAcAPAiijunT75L2XAi2vlNkzbpkxzH1MFQ0ImPIc19c-vopV2SgvffL-UObidVSSAh-eSbX98keUngnAAVH6wKg0PIoaKPkhlhvMxYKfjjZAaQiwwELY-SZ97fAkBBOHuaHBFW5gKKfJZ8vNigT1Xt0YbUYe9w7MWRVLfK-7Qzae-6gI1Nw8Z1vrGY9jed729UUB798-SJUa3HF7v2OPn56eJ68SW7-vb5cjG_ynTJWMhqyDmW1GhaKiCGUYbIBDBNYjXx5HRp8qpYMqixQKM1GEOhMBViTpDX9Dh5s40bT3M3oA9y3XiNbassdoOXnNGCV4xClGf_loSKiufFfyERoiqYIBGe_AFvu8HZeF2ZAytIxVke0ekWrVSLsrGmC07pMaKcE8EFAU5GlU2oFVp0qu0smiYOH_iTCa_75k4-ROcTKJYlrhs9GfXtwYJoAv4OKzV4Ly9_fD-07_5u59e_Fl8ntY654h0a2btmrdxGEpBjtsoH2Rr1q93DDvUal3u7S88IXu-A8lq1ximrG793BaXxK8dA77fOxym7Qrf_oal97wE92vvJ</recordid><startdate>20031120</startdate><enddate>20031120</enddate><creator>Rayapureddi, Jayanagendra P.</creator><creator>Kattamuri, Chandramohan</creator><creator>Steinmetz, Brian D.</creator><creator>Frankfort, Benjamin J.</creator><creator>Ostrin, Edwin J.</creator><creator>Mardon, Graeme</creator><creator>Hegde, Rashmi S.</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ATWCN</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7X8</scope><scope>7SC</scope><scope>7SP</scope><scope>7SR</scope><scope>7TB</scope><scope>7U5</scope><scope>8BQ</scope><scope>F28</scope><scope>JG9</scope><scope>JQ2</scope><scope>KR7</scope><scope>L7M</scope><scope>L~C</scope><scope>L~D</scope></search><sort><creationdate>20031120</creationdate><title>Eyes absent represents a class of protein tyrosine phosphatases</title><author>Rayapureddi, Jayanagendra P. ; Kattamuri, Chandramohan ; Steinmetz, Brian D. ; Frankfort, Benjamin J. ; Ostrin, Edwin J. ; Mardon, Graeme ; Hegde, Rashmi S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cataracts</topic><topic>Cell differentiation, maturation, development, hematopoiesis</topic><topic>Cell physiology</topic><topic>Drosophila melanogaster - embryology</topic><topic>Drosophila melanogaster - enzymology</topic><topic>Drosophila melanogaster - genetics</topic><topic>Drosophila Proteins - antagonists & inhibitors</topic><topic>Drosophila Proteins - chemistry</topic><topic>Drosophila Proteins - metabolism</topic><topic>Eye - embryology</topic><topic>Eye - enzymology</topic><topic>Eye - metabolism</topic><topic>Eye Proteins - antagonists & inhibitors</topic><topic>Eye Proteins - chemistry</topic><topic>Eye Proteins - metabolism</topic><topic>Eyes & eyesight</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humanities and Social Sciences</topic><topic>letter</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>multidisciplinary</topic><topic>Mutation</topic><topic>Phosphorylation</topic><topic>Protein Tyrosine Phosphatases - antagonists & inhibitors</topic><topic>Protein Tyrosine Phosphatases - chemistry</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Proteins</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rayapureddi, Jayanagendra P.</creatorcontrib><creatorcontrib>Kattamuri, Chandramohan</creatorcontrib><creatorcontrib>Steinmetz, Brian D.</creatorcontrib><creatorcontrib>Frankfort, Benjamin J.</creatorcontrib><creatorcontrib>Ostrin, Edwin J.</creatorcontrib><creatorcontrib>Mardon, Graeme</creatorcontrib><creatorcontrib>Hegde, Rashmi S.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Middle School</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Earth, Atmospheric & Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>Biological Sciences</collection><collection>Agriculture Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>ProQuest Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing & Allied Health Premium</collection><collection>ProQuest advanced technologies & aerospace journals</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric & Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest One Psychology</collection><collection>Engineering collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>SIRS Editorial</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Computer and Information Systems Abstracts</collection><collection>Electronics & Communications Abstracts</collection><collection>Engineered Materials Abstracts</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>METADEX</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Materials Research Database</collection><collection>ProQuest Computer Science Collection</collection><collection>Civil Engineering Abstracts</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>Computer and Information Systems Abstracts – Academic</collection><collection>Computer and Information Systems Abstracts Professional</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Rayapureddi, Jayanagendra P.</au><au>Kattamuri, Chandramohan</au><au>Steinmetz, Brian D.</au><au>Frankfort, Benjamin J.</au><au>Ostrin, Edwin J.</au><au>Mardon, Graeme</au><au>Hegde, Rashmi S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Eyes absent represents a class of protein tyrosine phosphatases</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2003-11-20</date><risdate>2003</risdate><volume>426</volume><issue>6964</issue><spage>295</spage><epage>298</epage><pages>295-298</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The Eyes absent proteins are members of a conserved regulatory network implicated in the development of the eye, muscle, kidney and ear
1
,
2
,
3
,
4
,
5
,
6
,
7
. Mutations in the Eyes absent genes have been associated with several congenital disorders including the multi-organ disease bronchio-oto-renal syndrome
8
, congenital cataracts
9
and late-onset deafness
10
. On the basis of previous analyses it has been shown that Eyes absent is a nuclear transcription factor, acting through interaction with homeodomain-containing Sine oculis (also known as Six) proteins
11
. Here we show that Eyes absent is also a protein tyrosine phosphatase. It does not resemble the classical tyrosine phosphatases that use cysteine as a nucleophile and proceed by means of a thiol-phosphate intermediate
12
. Rather, Eyes absent is the prototype for a class of protein tyrosine phosphatases that use a nucleophilic aspartic acid in a metal-dependent reaction. Furthermore, the phosphatase activity of Eyes absent contributes to its ability to induce eye formation in
Drosophila
.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>14628052</pmid><doi>10.1038/nature02093</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature (London), 2003-11, Vol.426 (6964), p.295-298 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743579430 |
| source | Nature |
| subjects | Amino Acid Sequence Animals Biological and medical sciences Cataracts Cell differentiation, maturation, development, hematopoiesis Cell physiology Drosophila melanogaster - embryology Drosophila melanogaster - enzymology Drosophila melanogaster - genetics Drosophila Proteins - antagonists & inhibitors Drosophila Proteins - chemistry Drosophila Proteins - metabolism Eye - embryology Eye - enzymology Eye - metabolism Eye Proteins - antagonists & inhibitors Eye Proteins - chemistry Eye Proteins - metabolism Eyes & eyesight Fundamental and applied biological sciences. Psychology Humanities and Social Sciences letter Molecular and cellular biology Molecular Sequence Data multidisciplinary Mutation Phosphorylation Protein Tyrosine Phosphatases - antagonists & inhibitors Protein Tyrosine Phosphatases - chemistry Protein Tyrosine Phosphatases - metabolism Proteins Science Science (multidisciplinary) Substrate Specificity |
| title | Eyes absent represents a class of protein tyrosine phosphatases |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-28T10%3A30%3A37IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Eyes%20absent%20represents%20a%20class%20of%20protein%20tyrosine%20phosphatases&rft.jtitle=Nature%20(London)&rft.au=Rayapureddi,%20Jayanagendra%20P.&rft.date=2003-11-20&rft.volume=426&rft.issue=6964&rft.spage=295&rft.epage=298&rft.pages=295-298&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/nature02093&rft_dat=%3Cgale_proqu%3EA187810712%3C/gale_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c644t-b027e63fc36a01f434ee4804c14c1f0933df295d40be5efcc0ff305f9ee21e7b3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=204519742&rft_id=info:pmid/14628052&rft_galeid=A187810712&rfr_iscdi=true |