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Open Access Green as soon as Postprint is submitted to ZB.
Formin-like 1 (FMNL1) is regulated by N-terminal myristoylation and induces polarized membrane blebbing.
J. Biol. Chem. 284, 33409-33417 (2009)
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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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
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
Volume: 284,
Issue: 48,
Pages: 33409-33417
Publisher
American Society for Biochemistry and Molecular Biology
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Molecular Immunology (IMI)