Loading…
Raver1, a dual compartment protein, is a ligand for PTB/hnRNP1 and microfilament attachment proteins
By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complex...
Saved in:
Published in: | The Journal of cell biology 2001-11, Vol.155 (5), p.775-785 |
---|---|
Main Authors: | , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
cited_by | |
---|---|
cites | |
container_end_page | 785 |
container_issue | 5 |
container_start_page | 775 |
container_title | The Journal of cell biology |
container_volume | 155 |
creator | Huettelmaier, S Illenberger, S Grosheva, I Ruediger, M Singer, R H Jockusch, B M |
description | By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complexes with the microfilament-associated proteins vinculin, metavinculin, and alpha -actinin and colocalizes with vinculin/metavinculin and alpha -actinin at microfilament attachment sites, such as cell-cell and cell matrix contacts of epithelial cells and fibroblasts, respectively, and in costameres of skeletal muscle. The NH sub(2)-terminal part of raver1 contains three RNA recognition motifs with homology to members of the heterogeneous nuclear RNP (hnRNP) family. Raver1 colocalizes with polypyrimidine tract binding protein (PTB)/hnRNPI, a protein involved in RNA splicing of microfilament proteins, in the perinucleolar compartment and forms complexes with PTB/hnRNPI. Hence, raver1 is a dual compartment protein, which is consistent with the presence of nuclear location signal and nuclear export sequence motifs in its sequence. During muscle differentiation, raver1 migrates from the nucleus to the costamere. We propose that raver1 may coordinate RNA processing and targeting as required for microfilament anchoring in specific adhesion sites. |
doi_str_mv | 10.1083/jcb.200105044 |
format | article |
fullrecord | <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_18257136</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>18257136</sourcerecordid><originalsourceid>FETCH-proquest_miscellaneous_182571363</originalsourceid><addsrcrecordid>eNqNjLkOwjAQRF2AxFnSu6JKwjoHRwsCUSGE6NHiOMSRY4Pt8P0EREFJNdKbN0PIhEHEYJnMKn6NYgAGGaRph_QBYhausjjrkYFzFQCkizTpk_yET2FZQJHmDSrKTX1H62uhPb1b44XUAZWurZW8oc5pYSw9ntezUp8OR0bfqJbcmkIq_KzQe-Tl74EbkW6ByonxN4dkutueN_uwFR6NcP5SS8eFUqiFadyFLeNswZJ58rf4Ag3rTK8</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>18257136</pqid></control><display><type>article</type><title>Raver1, a dual compartment protein, is a ligand for PTB/hnRNP1 and microfilament attachment proteins</title><source>Alma/SFX Local Collection</source><creator>Huettelmaier, S ; Illenberger, S ; Grosheva, I ; Ruediger, M ; Singer, R H ; Jockusch, B M</creator><creatorcontrib>Huettelmaier, S ; Illenberger, S ; Grosheva, I ; Ruediger, M ; Singer, R H ; Jockusch, B M</creatorcontrib><description>By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complexes with the microfilament-associated proteins vinculin, metavinculin, and alpha -actinin and colocalizes with vinculin/metavinculin and alpha -actinin at microfilament attachment sites, such as cell-cell and cell matrix contacts of epithelial cells and fibroblasts, respectively, and in costameres of skeletal muscle. The NH sub(2)-terminal part of raver1 contains three RNA recognition motifs with homology to members of the heterogeneous nuclear RNP (hnRNP) family. Raver1 colocalizes with polypyrimidine tract binding protein (PTB)/hnRNPI, a protein involved in RNA splicing of microfilament proteins, in the perinucleolar compartment and forms complexes with PTB/hnRNPI. Hence, raver1 is a dual compartment protein, which is consistent with the presence of nuclear location signal and nuclear export sequence motifs in its sequence. During muscle differentiation, raver1 migrates from the nucleus to the costamere. We propose that raver1 may coordinate RNA processing and targeting as required for microfilament anchoring in specific adhesion sites.</description><identifier>ISSN: 0021-9525</identifier><identifier>DOI: 10.1083/jcb.200105044</identifier><language>eng</language><subject>costameres ; hnRNPI protein ; metavinculin ; polypyrimidine tract-binding protein ; raver1 protein ; vinculin</subject><ispartof>The Journal of cell biology, 2001-11, Vol.155 (5), p.775-785</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids></links><search><creatorcontrib>Huettelmaier, S</creatorcontrib><creatorcontrib>Illenberger, S</creatorcontrib><creatorcontrib>Grosheva, I</creatorcontrib><creatorcontrib>Ruediger, M</creatorcontrib><creatorcontrib>Singer, R H</creatorcontrib><creatorcontrib>Jockusch, B M</creatorcontrib><title>Raver1, a dual compartment protein, is a ligand for PTB/hnRNP1 and microfilament attachment proteins</title><title>The Journal of cell biology</title><description>By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complexes with the microfilament-associated proteins vinculin, metavinculin, and alpha -actinin and colocalizes with vinculin/metavinculin and alpha -actinin at microfilament attachment sites, such as cell-cell and cell matrix contacts of epithelial cells and fibroblasts, respectively, and in costameres of skeletal muscle. The NH sub(2)-terminal part of raver1 contains three RNA recognition motifs with homology to members of the heterogeneous nuclear RNP (hnRNP) family. Raver1 colocalizes with polypyrimidine tract binding protein (PTB)/hnRNPI, a protein involved in RNA splicing of microfilament proteins, in the perinucleolar compartment and forms complexes with PTB/hnRNPI. Hence, raver1 is a dual compartment protein, which is consistent with the presence of nuclear location signal and nuclear export sequence motifs in its sequence. During muscle differentiation, raver1 migrates from the nucleus to the costamere. We propose that raver1 may coordinate RNA processing and targeting as required for microfilament anchoring in specific adhesion sites.</description><subject>costameres</subject><subject>hnRNPI protein</subject><subject>metavinculin</subject><subject>polypyrimidine tract-binding protein</subject><subject>raver1 protein</subject><subject>vinculin</subject><issn>0021-9525</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNqNjLkOwjAQRF2AxFnSu6JKwjoHRwsCUSGE6NHiOMSRY4Pt8P0EREFJNdKbN0PIhEHEYJnMKn6NYgAGGaRph_QBYhausjjrkYFzFQCkizTpk_yET2FZQJHmDSrKTX1H62uhPb1b44XUAZWurZW8oc5pYSw9ntezUp8OR0bfqJbcmkIq_KzQe-Tl74EbkW6ByonxN4dkutueN_uwFR6NcP5SS8eFUqiFadyFLeNswZJ58rf4Ag3rTK8</recordid><startdate>20011126</startdate><enddate>20011126</enddate><creator>Huettelmaier, S</creator><creator>Illenberger, S</creator><creator>Grosheva, I</creator><creator>Ruediger, M</creator><creator>Singer, R H</creator><creator>Jockusch, B M</creator><scope>7TM</scope></search><sort><creationdate>20011126</creationdate><title>Raver1, a dual compartment protein, is a ligand for PTB/hnRNP1 and microfilament attachment proteins</title><author>Huettelmaier, S ; Illenberger, S ; Grosheva, I ; Ruediger, M ; Singer, R H ; Jockusch, B M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_miscellaneous_182571363</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>costameres</topic><topic>hnRNPI protein</topic><topic>metavinculin</topic><topic>polypyrimidine tract-binding protein</topic><topic>raver1 protein</topic><topic>vinculin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Huettelmaier, S</creatorcontrib><creatorcontrib>Illenberger, S</creatorcontrib><creatorcontrib>Grosheva, I</creatorcontrib><creatorcontrib>Ruediger, M</creatorcontrib><creatorcontrib>Singer, R H</creatorcontrib><creatorcontrib>Jockusch, B M</creatorcontrib><collection>Nucleic Acids Abstracts</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Huettelmaier, S</au><au>Illenberger, S</au><au>Grosheva, I</au><au>Ruediger, M</au><au>Singer, R H</au><au>Jockusch, B M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Raver1, a dual compartment protein, is a ligand for PTB/hnRNP1 and microfilament attachment proteins</atitle><jtitle>The Journal of cell biology</jtitle><date>2001-11-26</date><risdate>2001</risdate><volume>155</volume><issue>5</issue><spage>775</spage><epage>785</epage><pages>775-785</pages><issn>0021-9525</issn><abstract>By screening a yeast two-hybrid library with COOH-terminal fragments of vinculin/metavinculin as the bait, we identified a new protein termed raver1. Raver1 is an 80-kD multidomain protein and widely expressed but to varying amounts in different cell lines. In situ and in vitro, raver1 forms complexes with the microfilament-associated proteins vinculin, metavinculin, and alpha -actinin and colocalizes with vinculin/metavinculin and alpha -actinin at microfilament attachment sites, such as cell-cell and cell matrix contacts of epithelial cells and fibroblasts, respectively, and in costameres of skeletal muscle. The NH sub(2)-terminal part of raver1 contains three RNA recognition motifs with homology to members of the heterogeneous nuclear RNP (hnRNP) family. Raver1 colocalizes with polypyrimidine tract binding protein (PTB)/hnRNPI, a protein involved in RNA splicing of microfilament proteins, in the perinucleolar compartment and forms complexes with PTB/hnRNPI. Hence, raver1 is a dual compartment protein, which is consistent with the presence of nuclear location signal and nuclear export sequence motifs in its sequence. During muscle differentiation, raver1 migrates from the nucleus to the costamere. We propose that raver1 may coordinate RNA processing and targeting as required for microfilament anchoring in specific adhesion sites.</abstract><doi>10.1083/jcb.200105044</doi></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0021-9525 |
ispartof | The Journal of cell biology, 2001-11, Vol.155 (5), p.775-785 |
issn | 0021-9525 |
language | eng |
recordid | cdi_proquest_miscellaneous_18257136 |
source | Alma/SFX Local Collection |
subjects | costameres hnRNPI protein metavinculin polypyrimidine tract-binding protein raver1 protein vinculin |
title | Raver1, a dual compartment protein, is a ligand for PTB/hnRNP1 and microfilament attachment proteins |
url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-23T03%3A22%3A00IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Raver1,%20a%20dual%20compartment%20protein,%20is%20a%20ligand%20for%20PTB/hnRNP1%20and%20microfilament%20attachment%20proteins&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Huettelmaier,%20S&rft.date=2001-11-26&rft.volume=155&rft.issue=5&rft.spage=775&rft.epage=785&rft.pages=775-785&rft.issn=0021-9525&rft_id=info:doi/10.1083/jcb.200105044&rft_dat=%3Cproquest%3E18257136%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-proquest_miscellaneous_182571363%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=18257136&rft_id=info:pmid/&rfr_iscdi=true |