Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
30
|
| pubmed:dateCreated |
1998-8-20
|
| pubmed:databankReference | |
| pubmed:abstractText |
We purified from rat brain a novel F-actin-binding protein with a Mr of about 105,000 (p105), which was estimated by SDS-polyacrylamide gel electrophoresis. We cloned its cDNA from a rat brain cDNA library and characterized it. p105 was a protein of 766 amino acids and showed a calculated Mr of 86,449. p105 consisted of one F-actin-binding domain at the N-terminal region, one Dbl homology domain and one pleckstrin homology domain at the middle region, and one cysteine-rich domain at the C-terminal region. This domain organization of p105 was similar to that of FGD1, which has been determined to be the genetic locus responsible for faciogenital dysplasia or Aarskog-Scott syndrome. We therefore named p105 frabin (FGD1-related F-actin-binding protein). Frabin bound along the sides of F-actin and showed F-actin-cross-linking activity. Overexpression of frabin in Swiss 3T3 cells and COS7 cells induced cell shape change and c-Jun N-terminal kinase activation, respectively, as described for FGD1. Because FGD1 has been shown to serve as a GDP/GTP exchange protein for Cdc42 small G protein, it is likely that frabin is a direct linker between Cdc42 and the actin cytoskeleton.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/JNK Mitogen-Activated Protein...,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
24
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
18697-700
|
| pubmed:dateRevised |
2009-11-19
|
| pubmed:meshHeading |
pubmed-meshheading:9668039-Actins,
pubmed-meshheading:9668039-Amino Acid Sequence,
pubmed-meshheading:9668039-Animals,
pubmed-meshheading:9668039-Brain Chemistry,
pubmed-meshheading:9668039-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:9668039-Cell Size,
pubmed-meshheading:9668039-Cells, Cultured,
pubmed-meshheading:9668039-Cloning, Molecular,
pubmed-meshheading:9668039-Enzyme Activation,
pubmed-meshheading:9668039-Female,
pubmed-meshheading:9668039-JNK Mitogen-Activated Protein Kinases,
pubmed-meshheading:9668039-Microfilament Proteins,
pubmed-meshheading:9668039-Mitogen-Activated Protein Kinases,
pubmed-meshheading:9668039-Molecular Sequence Data,
pubmed-meshheading:9668039-Molecular Weight,
pubmed-meshheading:9668039-Pregnancy,
pubmed-meshheading:9668039-Rabbits,
pubmed-meshheading:9668039-Rats
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Frabin, a novel FGD1-related actin filament-binding protein capable of changing cell shape and activating c-Jun N-terminal kinase.
|
| pubmed:affiliation |
Takai Biotimer Project, ERATO, Japan Science and Technology Corporation, c/o JCR Pharmaceuticals Co., Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan.
|
| pubmed:publicationType |
Journal Article
|