Loading…

The cytosolic splicing variant of NELL2 inhibits PKC beta 1 in glial cells

NELL2 is an abundant glycoprotein containing EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-spe...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 2014-11, Vol.454 (3), p.459-464
Main Authors: Lee, Da Yong, Kim, Eunju, Lee, Young-Sun, Ryu, Hwani, Park, Jae-Yong, Hwang, Eun Mi
Format: Article
Language:English
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by
cites
container_end_page 464
container_issue 3
container_start_page 459
container_title Biochemical and biophysical research communications
container_volume 454
creator Lee, Da Yong
Kim, Eunju
Lee, Young-Sun
Ryu, Hwani
Park, Jae-Yong
Hwang, Eun Mi
description NELL2 is an abundant glycoprotein containing EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-specific variant and the other is cytosolic NELL2 (cNELL2) which is non-secreted splicing variant of NELL2. Although cNELL2 structure was well characterized, the expression pattern or the cellular function of cNELL2 is not fully determined. In this study, we found that cNELL2 specifically interacts with PKC beta isotypes and inhibits PKC beta 1 through direct binding to the N-terminal pseudosubstrate domain of PKC beta 1. Here, we also demonstrate that cNELL2 is predominantly expressed and has inhibitory effects on the PKC downstream signaling pathways in astrocytes thereby establishing cNELL2 as an endogenous inhibitor of PKC beta 1 in glia.
doi_str_mv 10.1016/j.bbrc.2014.10.110
format article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_miscellaneous_1753469327</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1753469327</sourcerecordid><originalsourceid>FETCH-LOGICAL-p118t-819532f9ba281d0d6277ec45f0a985f3866f080fefb693521b2369d2255e1b2b3</originalsourceid><addsrcrecordid>eNotjz1PwzAYhD2ARCn8ASaPLAnva8eOPaKofEbAUCS2yk7s1lVIQuwi8e9JBcvd6RlOd4RcIeQIKG_2ubVTkzPAIj8yhBOyAACZMY0fZ-Q8xj0AYiH1gjytd442P2mIQxcaGsdZQ7-l32YKpk908PRlVdeMhn4XbEiRvj1X1LpkKM6MbrtgOtq4rosX5NSbLrrLf1-S97vVunrI6tf7x-q2zkZElTKFWnDmtTVMYQutZGXpmkJ4MFoJz5WUHhR4563UXDC0jEvdMiaEm7PlS3L91ztOw9fBxbT5DPG4wPRuOMQNloLP3zgr-S_oEk3e</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1753469327</pqid></control><display><type>article</type><title>The cytosolic splicing variant of NELL2 inhibits PKC beta 1 in glial cells</title><source>Elsevier</source><creator>Lee, Da Yong ; Kim, Eunju ; Lee, Young-Sun ; Ryu, Hwani ; Park, Jae-Yong ; Hwang, Eun Mi</creator><creatorcontrib>Lee, Da Yong ; Kim, Eunju ; Lee, Young-Sun ; Ryu, Hwani ; Park, Jae-Yong ; Hwang, Eun Mi</creatorcontrib><description>NELL2 is an abundant glycoprotein containing EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-specific variant and the other is cytosolic NELL2 (cNELL2) which is non-secreted splicing variant of NELL2. Although cNELL2 structure was well characterized, the expression pattern or the cellular function of cNELL2 is not fully determined. In this study, we found that cNELL2 specifically interacts with PKC beta isotypes and inhibits PKC beta 1 through direct binding to the N-terminal pseudosubstrate domain of PKC beta 1. Here, we also demonstrate that cNELL2 is predominantly expressed and has inhibitory effects on the PKC downstream signaling pathways in astrocytes thereby establishing cNELL2 as an endogenous inhibitor of PKC beta 1 in glia.</description><identifier>ISSN: 0006-291X</identifier><identifier>DOI: 10.1016/j.bbrc.2014.10.110</identifier><language>eng</language><ispartof>Biochemical and biophysical research communications, 2014-11, Vol.454 (3), p.459-464</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>314,780,784,27922,27923</link.rule.ids></links><search><creatorcontrib>Lee, Da Yong</creatorcontrib><creatorcontrib>Kim, Eunju</creatorcontrib><creatorcontrib>Lee, Young-Sun</creatorcontrib><creatorcontrib>Ryu, Hwani</creatorcontrib><creatorcontrib>Park, Jae-Yong</creatorcontrib><creatorcontrib>Hwang, Eun Mi</creatorcontrib><title>The cytosolic splicing variant of NELL2 inhibits PKC beta 1 in glial cells</title><title>Biochemical and biophysical research communications</title><description>NELL2 is an abundant glycoprotein containing EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-specific variant and the other is cytosolic NELL2 (cNELL2) which is non-secreted splicing variant of NELL2. Although cNELL2 structure was well characterized, the expression pattern or the cellular function of cNELL2 is not fully determined. In this study, we found that cNELL2 specifically interacts with PKC beta isotypes and inhibits PKC beta 1 through direct binding to the N-terminal pseudosubstrate domain of PKC beta 1. Here, we also demonstrate that cNELL2 is predominantly expressed and has inhibitory effects on the PKC downstream signaling pathways in astrocytes thereby establishing cNELL2 as an endogenous inhibitor of PKC beta 1 in glia.</description><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNotjz1PwzAYhD2ARCn8ASaPLAnva8eOPaKofEbAUCS2yk7s1lVIQuwi8e9JBcvd6RlOd4RcIeQIKG_2ubVTkzPAIj8yhBOyAACZMY0fZ-Q8xj0AYiH1gjytd442P2mIQxcaGsdZQ7-l32YKpk908PRlVdeMhn4XbEiRvj1X1LpkKM6MbrtgOtq4rosX5NSbLrrLf1-S97vVunrI6tf7x-q2zkZElTKFWnDmtTVMYQutZGXpmkJ4MFoJz5WUHhR4563UXDC0jEvdMiaEm7PlS3L91ztOw9fBxbT5DPG4wPRuOMQNloLP3zgr-S_oEk3e</recordid><startdate>20141121</startdate><enddate>20141121</enddate><creator>Lee, Da Yong</creator><creator>Kim, Eunju</creator><creator>Lee, Young-Sun</creator><creator>Ryu, Hwani</creator><creator>Park, Jae-Yong</creator><creator>Hwang, Eun Mi</creator><scope>7TK</scope></search><sort><creationdate>20141121</creationdate><title>The cytosolic splicing variant of NELL2 inhibits PKC beta 1 in glial cells</title><author>Lee, Da Yong ; Kim, Eunju ; Lee, Young-Sun ; Ryu, Hwani ; Park, Jae-Yong ; Hwang, Eun Mi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p118t-819532f9ba281d0d6277ec45f0a985f3866f080fefb693521b2369d2255e1b2b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lee, Da Yong</creatorcontrib><creatorcontrib>Kim, Eunju</creatorcontrib><creatorcontrib>Lee, Young-Sun</creatorcontrib><creatorcontrib>Ryu, Hwani</creatorcontrib><creatorcontrib>Park, Jae-Yong</creatorcontrib><creatorcontrib>Hwang, Eun Mi</creatorcontrib><collection>Neurosciences Abstracts</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lee, Da Yong</au><au>Kim, Eunju</au><au>Lee, Young-Sun</au><au>Ryu, Hwani</au><au>Park, Jae-Yong</au><au>Hwang, Eun Mi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The cytosolic splicing variant of NELL2 inhibits PKC beta 1 in glial cells</atitle><jtitle>Biochemical and biophysical research communications</jtitle><date>2014-11-21</date><risdate>2014</risdate><volume>454</volume><issue>3</issue><spage>459</spage><epage>464</epage><pages>459-464</pages><issn>0006-291X</issn><abstract>NELL2 is an abundant glycoprotein containing EGF-like domain in the neural tissues where it has multiple physiological functions by interacting with protein kinase C (PKC). There are two different splicing variant forms of NELL2 identified so far. One is secreted NELL2 (sNELL2) which is a neuron-specific variant and the other is cytosolic NELL2 (cNELL2) which is non-secreted splicing variant of NELL2. Although cNELL2 structure was well characterized, the expression pattern or the cellular function of cNELL2 is not fully determined. In this study, we found that cNELL2 specifically interacts with PKC beta isotypes and inhibits PKC beta 1 through direct binding to the N-terminal pseudosubstrate domain of PKC beta 1. Here, we also demonstrate that cNELL2 is predominantly expressed and has inhibitory effects on the PKC downstream signaling pathways in astrocytes thereby establishing cNELL2 as an endogenous inhibitor of PKC beta 1 in glia.</abstract><doi>10.1016/j.bbrc.2014.10.110</doi><tpages>6</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-291X
ispartof Biochemical and biophysical research communications, 2014-11, Vol.454 (3), p.459-464
issn 0006-291X
language eng
recordid cdi_proquest_miscellaneous_1753469327
source Elsevier
title The cytosolic splicing variant of NELL2 inhibits PKC beta 1 in glial cells
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T10%3A15%3A48IST&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=The%20cytosolic%20splicing%20variant%20of%20NELL2%20inhibits%20PKC%20beta%201%20in%20glial%20cells&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Lee,%20Da%20Yong&rft.date=2014-11-21&rft.volume=454&rft.issue=3&rft.spage=459&rft.epage=464&rft.pages=459-464&rft.issn=0006-291X&rft_id=info:doi/10.1016/j.bbrc.2014.10.110&rft_dat=%3Cproquest%3E1753469327%3C/proquest%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-p118t-819532f9ba281d0d6277ec45f0a985f3866f080fefb693521b2369d2255e1b2b3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=1753469327&rft_id=info:pmid/&rfr_iscdi=true