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Formin-like 1 (FMNL1) is regulated by N-terminal myristoylation and induces polarized membrane blebbing.

J. Biol. Chem. 284, 33409-33417 (2009)
DOI PMC
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
The formin protein formin-like 1 (FMNL1) is highly restrictedly expressed in hematopoietic lineage-derived cells and has been previously identified as a tumor-associated antigen. However, function and regulation of FMNL1 are not well defined. We have identified a novel splice variant (FMNL1 gamma) containing an intron retention at the C terminus affecting the diaphanous autoinhibitory domain (DAD). FMNL1 gamma is specifically located at the cell membrane and cortex in diverse cell lines. Similar localization of FMNL1 was observed for a mutant lacking the DAD domain (FMNL1 Delta DAD), indicating that deregulation of autoinhibition is effective in FMNL1 gamma. Expression of both FMNL1 gamma and FMNL1 Delta DAD induces polarized nonapoptotic blebbing that is dependent on N-terminal myristoylation of FMNL1 but independent of Src and ROCK activity. Thus, our results describe N-myristoylation as a regulative mechanism of FMNL1 responsible for membrane trafficking potentially involved in a diversity of polarized processes of hematopoietic lineage-derived cells.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Korrespondenzautor
Schlagwörter diaphanous-related formin; autoregulatory domain; actin-filaments; cell motility; mouse formin; FRL-alpha; protein; MDIA1; rho; identification
ISSN (print) / ISBN 0021-9258
e-ISSN 1083-351X
Quellenangaben Band: 284, Heft: 48, Seiten: 33409-33417 Artikelnummer: , Supplement: ,
Verlag American Society for Biochemistry and Molecular Biology
Nichtpatentliteratur Publikationen
Begutachtungsstatus Peer reviewed