rdf:type |
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lifeskim:mentions |
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pubmed:issue |
48
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pubmed:dateCreated |
2009-11-25
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pubmed:databankReference |
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pubmed:abstractText |
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 (FMNL1gamma) containing an intron retention at the C terminus affecting the diaphanous autoinhibitory domain (DAD). FMNL1gamma 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 (FMNL1DeltaDAD), indicating that deregulation of autoinhibition is effective in FMNL1gamma. Expression of both FMNL1gamma and FMNL1DeltaDAD 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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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/FMNL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Myristic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/ROCK1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/rho-Associated Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1083-351X
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pubmed:author |
|
pubmed:issnType |
Electronic
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pubmed:day |
27
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pubmed:volume |
284
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33409-17
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pubmed:dateRevised |
2011-3-3
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pubmed:meshHeading |
pubmed-meshheading:19815554-Alternative Splicing,
pubmed-meshheading:19815554-Binding Sites,
pubmed-meshheading:19815554-Cell Line,
pubmed-meshheading:19815554-Cell Line, Tumor,
pubmed-meshheading:19815554-Cell Membrane,
pubmed-meshheading:19815554-Cells, Cultured,
pubmed-meshheading:19815554-Cloning, Molecular,
pubmed-meshheading:19815554-Cytoskeletal Proteins,
pubmed-meshheading:19815554-DNA, Complementary,
pubmed-meshheading:19815554-Humans,
pubmed-meshheading:19815554-Immunoblotting,
pubmed-meshheading:19815554-K562 Cells,
pubmed-meshheading:19815554-Microscopy, Confocal,
pubmed-meshheading:19815554-Molecular Sequence Data,
pubmed-meshheading:19815554-Mutation,
pubmed-meshheading:19815554-Myristic Acid,
pubmed-meshheading:19815554-Protein Isoforms,
pubmed-meshheading:19815554-Protein Transport,
pubmed-meshheading:19815554-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:19815554-Sequence Analysis, DNA,
pubmed-meshheading:19815554-rho-Associated Kinases,
pubmed-meshheading:19815554-src-Family Kinases
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pubmed:year |
2009
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pubmed:articleTitle |
Formin-like 1 (FMNL1) is regulated by N-terminal myristoylation and induces polarized membrane blebbing.
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pubmed:affiliation |
Helmholtz Zentrum München, National Research Center for Environment and Health, Institute of Molecular Immunology, Marchioninistrasse 25, 81377 Munich, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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