SPIN90-IRSp53 complex participates in Rac-induced membrane ruffling

SPIN90 is a key regulator of actin cytoskeletal organization. Using the BioGRID beta database (General Repository for Interaction Datasets), we identified IRSp53 as a binding partner of SPIN90, and confirmed the in vivo formation of a SPIN90–IRSp53 complex mediated through direct association of the...

Full description

Saved in:
Bibliographic Details
Published in:Experimental cell research 2009-08, Vol.315 (14), p.2410-2419
Main Authors: Teodorof, Carmen, Bae, Jeom Il, Kim, Seon-Myung, Oh, Hye Jin, Kang, Yong Seok, Choi, Jeonghoon, Chun, Jang-Soo, Song, Woo Keun
Format: Article
Language:English
Subjects:
Actin
Adaptor Proteins, Signal Transducing - genetics
Adaptor Proteins, Signal Transducing - metabolism
Animals
Binding sites
Cell Membrane - metabolism
Cell Membrane - ultrastructure
Cell Movement - physiology
Cell Surface Extensions
Cellular biology
Cercopithecus aethiops
COS Cells
Cytoskeleton
Gene Knockdown Techniques
Genetic Vectors - metabolism
Humans
IRSp53
Membrane ruffling
Membranes
Muscle Proteins - genetics
Muscle Proteins - metabolism
Nerve Tissue Proteins - metabolism
Platelet-Derived Growth Factor - pharmacology
Proteins
rac GTP-Binding Proteins - metabolism
Rac1
RNA, Small Interfering - metabolism
SPIN90
Transfection
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!
Description
Summary:SPIN90 is a key regulator of actin cytoskeletal organization. Using the BioGRID beta database (General Repository for Interaction Datasets), we identified IRSp53 as a binding partner of SPIN90, and confirmed the in vivo formation of a SPIN90–IRSp53 complex mediated through direct association of the proline-rich domain (PRD) of SPIN90 with the SH3 domain of IRSp53. SPIN90 and IRSp53 positively cooperated to mediate Rac activation, and co-expression of SPIN90 and IRSp53 in COS-7 cells led to the complex formation of SPIN90-IRSp53 in the leading edge of cells. PDGF treatment induced strong colocalization of SPIN90 and IRSp53 at membrane protrusions. Within such PDGF-induced protrusions, knockdown of SPIN90 protein using siRNA significantly reduced lamellipodia-like protrusions as well as localization of IRSp53 at those sites. Finally, competitive inhibition of SPIN90-IRSp53 binding by SPIN90 PRD dramatically reduced ruffle formation, further suggesting that SPIN90 plays a key role in the formation of the membrane protrusions associated with cell motility.
ISSN:0014-4827
1090-2422
DOI:10.1016/j.yexcr.2009.05.010