期刊
BIOCHEMICAL JOURNAL
卷 473, 期 -, 页码 383-396出版社
PORTLAND PRESS LTD
DOI: 10.1042/BJ20151050
关键词
actin; cross-linking; kinetics; nucleation; polymerization
资金
- National Center for Research Resources [5P20RR017708]
- COBRE grant from the National Institute of General Medical Sciences at the National Institutes of Health [8P20GM103420]
- Burroughs-Wellcome Trust Collaborative Grant
- Flossie E. West Memorial Foundation Trust
- Wichita State University
- Institutional Development Award (IDeA) from the National Institute of General Medical Sciences at the National Institutes of Health [P20GM103418]
The actin scaffold protein palladin regulates both normal cell migration and invasive cell motility, processes that require the co-ordinated regulation of actin dynamics. However, the potential effect of palladin on actin dynamics has remained elusive. In the present study, we show that the actin-binding immunoglobulin-like domain of palladin, which is directly responsible for both actin binding and bundling, also stimulates actin polymerization in vitro. Palladin eliminated the lag phase that is characteristic of the slow nucleation step of actin polymerization. Furthermore, palladin dramatically reduced depolymerization, slightly enhanced the elongation rate, and did not alter the critical concentration. Microscopy and in vitro crosslinking assays reveal differences in actin bundle architecture when palladin is incubated with actin before or after polymerization. These results suggest a model whereby palladin stimulates a polymerization-competent form of globular or monomeric actin (G-actin), akin to metal ions, either through charge neutralization or through conformational changes.
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