Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction

Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila...

Full description

Saved in:
Bibliographic Details
Published in:Biology open 2014-12, Vol.3 (12), p.1196-1206
Main Authors: Wang, Simon Ji Hau, Tsai, Amy, Wang, Mannan, Yoo, SooHyun, Kim, Hae-Yoon, Yoo, Byoungjoo, Chui, Vincent, Kisiel, Marta, Stewart, Bryan, Parkhouse, Wade, Harden, Nicholas, Krieger, Charles
Format: Article
Language:English
Subjects:
Actin
Adducin
Alanine
Ca2+/calmodulin-dependent protein kinase II
Cytoskeleton
Dlg
Drosophila
Fruit flies
Homology
Hts
Insects
Isoforms
Kinases
MARCKS protein
Muscles
Neuromuscular junction
Neuromuscular junctions
Phosphatidylinositol 4,5-diphosphate
Phosphorylation
PIP2
Plasticity
Protein kinase C
Proteinase-activated receptor 1
Proteins
Spectrin
Synaptic plasticity
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-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903
cites cdi_FETCH-LOGICAL-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903
container_end_page 1206
container_issue 12
container_start_page 1196
container_title Biology open
container_volume 3
creator Wang, Simon Ji Hau
Tsai, Amy
Wang, Mannan
Yoo, SooHyun
Kim, Hae-Yoon
Yoo, Byoungjoo
Chui, Vincent
Kisiel, Marta
Stewart, Bryan
Parkhouse, Wade
Harden, Nicholas
Krieger, Charles
description Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila adducin, Hu-li tai shao (Hts), plays a role in larval neuromuscular junction (NMJ) growth. Here, we find that the predominant isoforms of Hts at the NMJ contain the MARCKS-homology domain, which is important for interactions with Discs large (Dlg) and phosphatidylinositol 4,5-bisphosphate (PIP2). Through the use of Proximity Ligation Assay (PLA), we show that the adducin-like Hts isoforms are in complexes with Dlg and PIP2 at the NMJ. We provide evidence that Hts promotes the phosphorylation and delocalization of Dlg at the NMJ through regulation of the transcript distribution of the PAR-1 and CaMKII kinases in the muscle. We also show that Hts interactions with Dlg and PIP2 are impeded through phosphorylation of the MARCKS-homology domain. These results are further evidence that Hts is a signaling-responsive regulator of synaptic plasticity in Drosophila.
doi_str_mv 10.1242/bio.20148342
format article
fullrecord <record><control><sourceid>proquest_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_2765a2602f5d4626bda471ceba2f2b5a</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><doaj_id>oai_doaj_org_article_2765a2602f5d4626bda471ceba2f2b5a</doaj_id><sourcerecordid>1637572015</sourcerecordid><originalsourceid>FETCH-LOGICAL-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903</originalsourceid><addsrcrecordid>eNqFks1vFCEYxidGY5vam2dD4sWDW4EZYOZiYlo_NmniHvRMXhhmhw0DIzDV_S_8k2Xdtmm9yOXl45cHnpenql4SfEFoQ98pGy4oJk1bN_RJdUpxw1e87vDTB_OT6jylHS6DY8a7-nl1QllDeFmeVr83Y0jzGFbRbBcH2fToKoYU5tE6QND3i7Ye2YQA9SabOFkPPqMwoLT3MGer0ewglWrzHhUUkA7T7Mwv9NPmEV25LQLfo816QxFklEeDHMQbcMibJYZpSbrcG9Fu8Trb4F9UzwZwyZzf1rPq-6eP3y6_rK6_fl5ffrheaUZILsYEI7Q2hrXaMGOGmvaatQoLMYiGE8VJPVBBVAeq7lpimNJKEGLarutUh-uzan3U7QPs5BztBHEvA1j5dyPErYRYbDkjqeAMKMd0YH3DKVc9NIJoo4AOVDEoWu-PWvOiJtNr43ME90j08Ym3o9yGG9lQzgQTReDNrUAMPxaTspxs0sY58CYsSZIWt4JiUdP_o4fOFJawgr7-B92FJfrS1YMl0rUtFwfq7ZHS5d9TNMP9uwmWh5DJEjJ5F7KCv3ro9R6-i1T9BzFWzjw</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2761988675</pqid></control><display><type>article</type><title>Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction</title><source>Publicly Available Content Database (Proquest) (PQ_SDU_P3)</source><source>PubMed Central</source><creator>Wang, Simon Ji Hau ; Tsai, Amy ; Wang, Mannan ; Yoo, SooHyun ; Kim, Hae-Yoon ; Yoo, Byoungjoo ; Chui, Vincent ; Kisiel, Marta ; Stewart, Bryan ; Parkhouse, Wade ; Harden, Nicholas ; Krieger, Charles</creator><creatorcontrib>Wang, Simon Ji Hau ; Tsai, Amy ; Wang, Mannan ; Yoo, SooHyun ; Kim, Hae-Yoon ; Yoo, Byoungjoo ; Chui, Vincent ; Kisiel, Marta ; Stewart, Bryan ; Parkhouse, Wade ; Harden, Nicholas ; Krieger, Charles</creatorcontrib><description>Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila adducin, Hu-li tai shao (Hts), plays a role in larval neuromuscular junction (NMJ) growth. Here, we find that the predominant isoforms of Hts at the NMJ contain the MARCKS-homology domain, which is important for interactions with Discs large (Dlg) and phosphatidylinositol 4,5-bisphosphate (PIP2). Through the use of Proximity Ligation Assay (PLA), we show that the adducin-like Hts isoforms are in complexes with Dlg and PIP2 at the NMJ. We provide evidence that Hts promotes the phosphorylation and delocalization of Dlg at the NMJ through regulation of the transcript distribution of the PAR-1 and CaMKII kinases in the muscle. We also show that Hts interactions with Dlg and PIP2 are impeded through phosphorylation of the MARCKS-homology domain. These results are further evidence that Hts is a signaling-responsive regulator of synaptic plasticity in Drosophila.</description><identifier>ISSN: 2046-6390</identifier><identifier>EISSN: 2046-6390</identifier><identifier>DOI: 10.1242/bio.20148342</identifier><identifier>PMID: 25416060</identifier><language>eng</language><publisher>England: The Company of Biologists</publisher><subject>Actin ; Adducin ; Alanine ; Ca2+/calmodulin-dependent protein kinase II ; Cytoskeleton ; Dlg ; Drosophila ; Fruit flies ; Homology ; Hts ; Insects ; Isoforms ; Kinases ; MARCKS protein ; Muscles ; Neuromuscular junction ; Neuromuscular junctions ; Phosphatidylinositol 4,5-diphosphate ; Phosphorylation ; PIP2 ; Plasticity ; Protein kinase C ; Proteinase-activated receptor 1 ; Proteins ; Spectrin ; Synaptic plasticity</subject><ispartof>Biology open, 2014-12, Vol.3 (12), p.1196-1206</ispartof><rights>2014. Published by The Company of Biologists Ltd.</rights><rights>2014. This work is licensed under https://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014. Published by The Company of Biologists Ltd 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903</citedby><cites>FETCH-LOGICAL-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4265757/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2761988675?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25416060$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Wang, Simon Ji Hau</creatorcontrib><creatorcontrib>Tsai, Amy</creatorcontrib><creatorcontrib>Wang, Mannan</creatorcontrib><creatorcontrib>Yoo, SooHyun</creatorcontrib><creatorcontrib>Kim, Hae-Yoon</creatorcontrib><creatorcontrib>Yoo, Byoungjoo</creatorcontrib><creatorcontrib>Chui, Vincent</creatorcontrib><creatorcontrib>Kisiel, Marta</creatorcontrib><creatorcontrib>Stewart, Bryan</creatorcontrib><creatorcontrib>Parkhouse, Wade</creatorcontrib><creatorcontrib>Harden, Nicholas</creatorcontrib><creatorcontrib>Krieger, Charles</creatorcontrib><title>Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction</title><title>Biology open</title><addtitle>Biol Open</addtitle><description>Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila adducin, Hu-li tai shao (Hts), plays a role in larval neuromuscular junction (NMJ) growth. Here, we find that the predominant isoforms of Hts at the NMJ contain the MARCKS-homology domain, which is important for interactions with Discs large (Dlg) and phosphatidylinositol 4,5-bisphosphate (PIP2). Through the use of Proximity Ligation Assay (PLA), we show that the adducin-like Hts isoforms are in complexes with Dlg and PIP2 at the NMJ. We provide evidence that Hts promotes the phosphorylation and delocalization of Dlg at the NMJ through regulation of the transcript distribution of the PAR-1 and CaMKII kinases in the muscle. We also show that Hts interactions with Dlg and PIP2 are impeded through phosphorylation of the MARCKS-homology domain. These results are further evidence that Hts is a signaling-responsive regulator of synaptic plasticity in Drosophila.</description><subject>Actin</subject><subject>Adducin</subject><subject>Alanine</subject><subject>Ca2+/calmodulin-dependent protein kinase II</subject><subject>Cytoskeleton</subject><subject>Dlg</subject><subject>Drosophila</subject><subject>Fruit flies</subject><subject>Homology</subject><subject>Hts</subject><subject>Insects</subject><subject>Isoforms</subject><subject>Kinases</subject><subject>MARCKS protein</subject><subject>Muscles</subject><subject>Neuromuscular junction</subject><subject>Neuromuscular junctions</subject><subject>Phosphatidylinositol 4,5-diphosphate</subject><subject>Phosphorylation</subject><subject>PIP2</subject><subject>Plasticity</subject><subject>Protein kinase C</subject><subject>Proteinase-activated receptor 1</subject><subject>Proteins</subject><subject>Spectrin</subject><subject>Synaptic plasticity</subject><issn>2046-6390</issn><issn>2046-6390</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNqFks1vFCEYxidGY5vam2dD4sWDW4EZYOZiYlo_NmniHvRMXhhmhw0DIzDV_S_8k2Xdtmm9yOXl45cHnpenql4SfEFoQ98pGy4oJk1bN_RJdUpxw1e87vDTB_OT6jylHS6DY8a7-nl1QllDeFmeVr83Y0jzGFbRbBcH2fToKoYU5tE6QND3i7Ye2YQA9SabOFkPPqMwoLT3MGer0ewglWrzHhUUkA7T7Mwv9NPmEV25LQLfo816QxFklEeDHMQbcMibJYZpSbrcG9Fu8Trb4F9UzwZwyZzf1rPq-6eP3y6_rK6_fl5ffrheaUZILsYEI7Q2hrXaMGOGmvaatQoLMYiGE8VJPVBBVAeq7lpimNJKEGLarutUh-uzan3U7QPs5BztBHEvA1j5dyPErYRYbDkjqeAMKMd0YH3DKVc9NIJoo4AOVDEoWu-PWvOiJtNr43ME90j08Ym3o9yGG9lQzgQTReDNrUAMPxaTspxs0sY58CYsSZIWt4JiUdP_o4fOFJawgr7-B92FJfrS1YMl0rUtFwfq7ZHS5d9TNMP9uwmWh5DJEjJ5F7KCv3ro9R6-i1T9BzFWzjw</recordid><startdate>20141215</startdate><enddate>20141215</enddate><creator>Wang, Simon Ji Hau</creator><creator>Tsai, Amy</creator><creator>Wang, Mannan</creator><creator>Yoo, SooHyun</creator><creator>Kim, Hae-Yoon</creator><creator>Yoo, Byoungjoo</creator><creator>Chui, Vincent</creator><creator>Kisiel, Marta</creator><creator>Stewart, Bryan</creator><creator>Parkhouse, Wade</creator><creator>Harden, Nicholas</creator><creator>Krieger, Charles</creator><general>The Company of Biologists</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PATMY</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PYCSY</scope><scope>7X8</scope><scope>7QO</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20141215</creationdate><title>Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction</title><author>Wang, Simon Ji Hau ; Tsai, Amy ; Wang, Mannan ; Yoo, SooHyun ; Kim, Hae-Yoon ; Yoo, Byoungjoo ; Chui, Vincent ; Kisiel, Marta ; Stewart, Bryan ; Parkhouse, Wade ; Harden, Nicholas ; Krieger, Charles</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Actin</topic><topic>Adducin</topic><topic>Alanine</topic><topic>Ca2+/calmodulin-dependent protein kinase II</topic><topic>Cytoskeleton</topic><topic>Dlg</topic><topic>Drosophila</topic><topic>Fruit flies</topic><topic>Homology</topic><topic>Hts</topic><topic>Insects</topic><topic>Isoforms</topic><topic>Kinases</topic><topic>MARCKS protein</topic><topic>Muscles</topic><topic>Neuromuscular junction</topic><topic>Neuromuscular junctions</topic><topic>Phosphatidylinositol 4,5-diphosphate</topic><topic>Phosphorylation</topic><topic>PIP2</topic><topic>Plasticity</topic><topic>Protein kinase C</topic><topic>Proteinase-activated receptor 1</topic><topic>Proteins</topic><topic>Spectrin</topic><topic>Synaptic plasticity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Wang, Simon Ji Hau</creatorcontrib><creatorcontrib>Tsai, Amy</creatorcontrib><creatorcontrib>Wang, Mannan</creatorcontrib><creatorcontrib>Yoo, SooHyun</creatorcontrib><creatorcontrib>Kim, Hae-Yoon</creatorcontrib><creatorcontrib>Yoo, Byoungjoo</creatorcontrib><creatorcontrib>Chui, Vincent</creatorcontrib><creatorcontrib>Kisiel, Marta</creatorcontrib><creatorcontrib>Stewart, Bryan</creatorcontrib><creatorcontrib>Parkhouse, Wade</creatorcontrib><creatorcontrib>Harden, Nicholas</creatorcontrib><creatorcontrib>Krieger, Charles</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Proquest Health &amp; Medical Complete</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest SciTech 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>ProQuest Central (Alumni)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central</collection><collection>Agricultural &amp; Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>PML(ProQuest Medical Library)</collection><collection>Biological Science Database</collection><collection>Environmental Science Database</collection><collection>Publicly Available Content Database (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Environmental Science Collection</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>Biology open</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Wang, Simon Ji Hau</au><au>Tsai, Amy</au><au>Wang, Mannan</au><au>Yoo, SooHyun</au><au>Kim, Hae-Yoon</au><au>Yoo, Byoungjoo</au><au>Chui, Vincent</au><au>Kisiel, Marta</au><au>Stewart, Bryan</au><au>Parkhouse, Wade</au><au>Harden, Nicholas</au><au>Krieger, Charles</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction</atitle><jtitle>Biology open</jtitle><addtitle>Biol Open</addtitle><date>2014-12-15</date><risdate>2014</risdate><volume>3</volume><issue>12</issue><spage>1196</spage><epage>1206</epage><pages>1196-1206</pages><issn>2046-6390</issn><eissn>2046-6390</eissn><abstract>Adducin is a ubiquitously expressed actin- and spectrin-binding protein involved in cytoskeleton organization, and is regulated through phosphorylation of the myristoylated alanine-rich C-terminal kinase (MARCKS)-homology domain by protein kinase C (PKC). We have previously shown that the Drosophila adducin, Hu-li tai shao (Hts), plays a role in larval neuromuscular junction (NMJ) growth. Here, we find that the predominant isoforms of Hts at the NMJ contain the MARCKS-homology domain, which is important for interactions with Discs large (Dlg) and phosphatidylinositol 4,5-bisphosphate (PIP2). Through the use of Proximity Ligation Assay (PLA), we show that the adducin-like Hts isoforms are in complexes with Dlg and PIP2 at the NMJ. We provide evidence that Hts promotes the phosphorylation and delocalization of Dlg at the NMJ through regulation of the transcript distribution of the PAR-1 and CaMKII kinases in the muscle. We also show that Hts interactions with Dlg and PIP2 are impeded through phosphorylation of the MARCKS-homology domain. These results are further evidence that Hts is a signaling-responsive regulator of synaptic plasticity in Drosophila.</abstract><cop>England</cop><pub>The Company of Biologists</pub><pmid>25416060</pmid><doi>10.1242/bio.20148342</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 2046-6390
ispartof Biology open, 2014-12, Vol.3 (12), p.1196-1206
issn 2046-6390
2046-6390
language eng
recordid cdi_doaj_primary_oai_doaj_org_article_2765a2602f5d4626bda471ceba2f2b5a
source Publicly Available Content Database (Proquest) (PQ_SDU_P3); PubMed Central
subjects Actin
Adducin
Alanine
Ca2+/calmodulin-dependent protein kinase II
Cytoskeleton
Dlg
Drosophila
Fruit flies
Homology
Hts
Insects
Isoforms
Kinases
MARCKS protein
Muscles
Neuromuscular junction
Neuromuscular junctions
Phosphatidylinositol 4,5-diphosphate
Phosphorylation
PIP2
Plasticity
Protein kinase C
Proteinase-activated receptor 1
Proteins
Spectrin
Synaptic plasticity
title Phospho-regulated Drosophila adducin is a determinant of synaptic plasticity in a complex with Dlg and PIP2 at the larval neuromuscular junction
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-10T13%3A27%3A35IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Phospho-regulated%20Drosophila%20adducin%20is%20a%20determinant%20of%20synaptic%20plasticity%20in%20a%20complex%20with%20Dlg%20and%20PIP2%20at%20the%20larval%20neuromuscular%20junction&rft.jtitle=Biology%20open&rft.au=Wang,%20Simon%20Ji%20Hau&rft.date=2014-12-15&rft.volume=3&rft.issue=12&rft.spage=1196&rft.epage=1206&rft.pages=1196-1206&rft.issn=2046-6390&rft.eissn=2046-6390&rft_id=info:doi/10.1242/bio.20148342&rft_dat=%3Cproquest_doaj_%3E1637572015%3C/proquest_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c511t-6375123ee58ce5eef32dc58b077f7461b613f271b9ab3981e5bcb711e8999b903%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=2761988675&rft_id=info:pmid/25416060&rfr_iscdi=true