The oligomeric status of syndecan-4 regulates syndecan-4 interaction with α-actinin-Reference-Cited by-同舟云学术

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The oligomeric status of syndecan-4 regulates syndecan-4 interaction with α-actinin

Published:2008-10 Issue:10 Volume:87 Page:807-815
ISSN:0171-9335
Container-title:European Journal of Cell Biology
language:en
Short-container-title:European Journal of Cell Biology

Author:

Choi Youngsil,Kim Seungin,Lee Junghyun,Ko Sung-gun,Lee Weontae,Han Inn-Oc,Woods Anne,Oh Eok-Soo

Publisher

Elsevier BV

Subject

Cell Biology,General Medicine,Histology,Pathology and Forensic Medicine

Reference26 articles.

1. Syndesmos, a protein that interacts with the cytoplasmic domain of syndecan-4, mediates cell spreading and actin cytoskeletal organization;Baciu;J. Cell Sci.,2000

2. Cytoplasmic interactions of syndecan-4 orchestrate adhesion receptor and growth factor receptor signaling;Bass;Biochem. J.,2002

3. Protein kinase Cdelta-dependent phosphorylation of syndecan-4 regulates cell migration;Chaudhuri;Circ. Res.,2005

4. Transmembrane domain-induced oligomerization is crucial for the functions of syndecan-2 and syndecan-4;Choi;J. Biol. Chem.,2005

5. PKCα-dependent activation of RhoA by syndecan-4 during focal adhesion formation;Dovas;J. Cell Sci.,2006

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4. Syndecan Transmembrane Domain Specifically Regulates Downstream Signaling Events of the Transmembrane Receptor Cytoplasmic Domain;International Journal of Molecular Sciences;2021-07-24

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