Swiprosin-1 modulates actin dynamics by regulating the F-actin accessibility to cofilinopen access
- Authors
- Huh, Yun Hyun; Kim, So Hee; Chung, Kyoung-Hwun; Oh, Sena; Kwon, Min-Sung; Choi, Hyun-Woo; Rhee, Sangmyung; Ryu, Je-Hwang; Park, Zee Yong; Jun, Chang-Duk; Song, Woo Keun
- Issue Date
- Dec-2013
- Publisher
- SPRINGER BASEL AG
- Keywords
- Swiprosin-1; Actin filament; Cofilin; Lamellipodia
- Citation
- CELLULAR AND MOLECULAR LIFE SCIENCES, v.70, no.24, pp 4841 - 4854
- Pages
- 14
- Journal Title
- CELLULAR AND MOLECULAR LIFE SCIENCES
- Volume
- 70
- Number
- 24
- Start Page
- 4841
- End Page
- 4854
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14063
- DOI
- 10.1007/s00018-013-1447-5
- ISSN
- 1420-682X
1420-9071
- Abstract
- Membrane protrusions, like lamellipodia, and cell movement are dependent on actin dynamics, which are regulated by a variety of actin-binding proteins acting cooperatively to reorganize actin filaments. Here, we provide evidence that Swiprosin-1, a newly identified actin-binding protein, modulates lamellipodial dynamics by regulating the accessibility of F-actin to cofilin. Overexpression of Swiprosin-1 increased lamellipodia formation in B16F10 melanoma cells, whereas knockdown of Swiprosin-1 inhibited EGF-induced lamellipodia formation, and led to a loss of actin stress fibers at the leading edges of cells but not in the cell cortex. Swiprosin-1 strongly facilitated the formation of entangled or clustered F-actin, which remodeled the structural organization of actin filaments making them inaccessible to cofilin. EGF-induced phosphorylation of Swiprosin-1 at Ser183, a phosphorylation site newly identified using mass spectrometry, effectively inhibited clustering of actin filaments and permitted cofilin access to F-actin, resulting in actin depolymerization. Cells overexpressing a Swiprosin-1 phosphorylation-mimicking mutant or a phosphorylation-deficient mutant exhibited irregular membrane dynamics during the protrusion and retraction cycles of lamellipodia. Taken together, these findings suggest that dynamic exchange of Swiprosin-1 phosphorylation and dephosphorylation is a novel mechanism that regulates actin dynamics by modulating the pattern of cofilin activity at the leading edges of cells.
- Files in This Item
-
- Appears in
Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14063)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.