期刊
BMC CELL BIOLOGY
卷 6, 期 -, 页码 -出版社
BIOMED CENTRAL LTD
DOI: 10.1186/1471-2121-6-45
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- NCRR NIH HHS [1S10RR107903-01] Funding Source: Medline
- NIEHS NIH HHS [P30 ES000210, P30 ES00210] Funding Source: Medline
- NIGMS NIH HHS [R01 GM063711, GM 63711] Funding Source: Medline
Background: Cysteine-rich protein I (CRPI) is a LIM domain containing protein localized to the nucleus and the actin cytoskeleton. CRPI has been demonstrated to bind the actin-bundling protein alpha-actinin and proposed to modulate the actin cytoskeleton; however, specific regulatory mechanisms have not been identified. Results: CRPI expression increased actin bundling in rat embryonic fibroblasts. Although CRPI did not affect the bundling activity of alpha-actinin, CRPI was found to stabilize the interaction of alpha-actinin with actin bundles and to directly bundle actin microfilaments. Using confocal and photobleaching fluorescence resonance energy transfer ( FRET) microscopy, we demonstrate that there are two populations of CRPI localized along actin stress fibers, one associated through interaction with alpha-actinin and one that appears to bind the actin filaments directly. Consistent with a role in regulating actin filament cross-linking, CRPI also localized to the membrane ruffles of spreading and PDGF treated fibroblasts. Conclusion: CRPI regulates actin filament bundling by directly cross-linking actin filaments and stabilizing the interaction of alpha-actinin with actin filament bundles.
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