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Dynamin II interacts with syndecan-4, a regulator of focal adhesion and stress-fiber formation

Title
Dynamin II interacts with syndecan-4, a regulator of focal adhesion and stress-fiber formation
Authors
Yoo J.Jeong M.-J.Cho H.J.Oh E.S.Han M.Y.
Ewha Authors
오억수
SCOPUS Author ID
오억수scopus
Issue Date
2005
Journal Title
Biochemical and Biophysical Research Communications
ISSN
0006-291XJCR Link
Citation
vol. 328, no. 2, pp. 424 - 431
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
Dynamin is a large mechanochemical GTPase that has been implicated in vesicle formation in multiple cellular compartments. It is believed that dynamin interacts with a variety of cellular proteins to constrict membranes. To identify potential intracellular proteins that interact with the PH domain of dynamin II, we carried out a yeast two-hybrid screen in which the PH domain of dynamin II was used as bait. The cell surface heparan sulfate proteoglycan syndecan-4 that acts in conjunction with integrins to promote the formation of actin stress fibers and focal adhesions was isolated as a binding partner for the PH domain of dynamin II. In vitro binding assays, immunoprecipitation, and confocal microscopy analysis confirmed the association of dynamin II with syndecan-4. Most dramatic finding of our study is that the cytoplasmic distribution of dynamin II and syndecan-4 changes in fibroblasts that have been stimulated to form the focal adhesions and stress fibers with LPA. In quiescent cells, dynamin II is evenly distributed in the cytoplasm and colocalizes with syndecan-4 near the nucleus. Upon treatment with LPA to induce focal adhesions and stress-fiber formation, dynamin II becomes markedly associated with syndecan-4 at focal adhesion sites. We further established the colocalization of syndecan-4 and dynamin with paxillin and actin as marker proteins for focal adhesions and stress fibers, respectively. All of these results suggest that the interaction between dynamin II and syndecan-4 is important in mediating focal adhesion and stress-fiber formation. © 2005 Elsevier Inc. All rights reserved.
DOI
10.1016/j.bbrc.2004.12.179
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자연과학대학 > 생명과학전공 > Journal papers
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