期刊
JOURNAL OF CELL SCIENCE
卷 120, 期 2, 页码 340-352出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.03335
关键词
filopodia; actin; cdc42; lipid phosphatase
类别
资金
- NCI NIH HHS [CA096496] Funding Source: Medline
- NIDCD NIH HHS [R01 DC003299, DC03299] Funding Source: Medline
- NIGMS NIH HHS [GM00678, GM54388] Funding Source: Medline
Fiilopodia are dynamic cell surface protrusions that are required for proper cellular development and function. We report that the integral membrane protein lipidphosphatase-related protein 1 (LPR1) localizes to and promotes the formation of actin-rich, dynamic filopodia, both along the cell periphery and the dorsal cell surface. Regulation of filopodia by LPR1 was not mediated by cdc42 or Rif, and is independent of the Arp2/3 complex. We found that LPR1 can induce filopodia formation in the absence of the Ena/Vasp family of proteins, suggesting that these molecules are not essential for the development of the protrusions. Mutagenesis experiments identified residues and regions of LPR1 that are important for the induction of filopodia. RNA interference experiments in an ovarian epithelial cancer cell line demonstrated a role for LPR1 in the maintenance of filopodia-like membrane protrusions. These observations, and our finding that LPR1 is a not an active lipid phosphatase, suggest that LPR1 may be a novel integral membrane protein link between the actin core and the surrounding lipid layer of a nascent filopodium.
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