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Direct interaction between metastasis‐associated protein 1 and endophilin 3
Author(s) -
Aramaki Yuko,
Ogawa Katsuhiro,
Toh Yasushi,
Ito Takahiro,
Akimitsu Nobuyoshi,
Hamamoto Hiroshi,
Sekimizu Kazuhisa,
Matsusue Kimihiko,
Kono Akira,
Iguchi Haruo,
Takiguchi Soichi
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.05.069
Subject(s) - cytoplasm , endocytosis , microbiology and biotechnology , two hybrid screening , immunoprecipitation , complementary dna , signal transducing adaptor protein , biology , chemistry , yeast , genetics , cell , gene , signal transduction
The yeast two‐hybrid system was used to search for partners of mouse metastasis‐associated protein 1 (Mta1). Screening of a cDNA library prepared from mouse embryo yielded positive clones coding for endophilin 3. The site of interaction was suggested to be the SH‐3‐binding domain of Mta1 and SH‐3 domain of endophilin 3. This interaction was confirmed by GST pull‐down assay in vitro and immunoprecipitation in vivo. The Mta1 and endophilin 3 transcripts were highly expressed in testis and brain. But, Mta1 localized mainly in nucleus and to a lesser extent in cytoplasm while endophilin 3 localized mainly in cytoplasm. If Mta1 functions in cytoplasm, it might be involved in the regulation of endocytosis mediated by endophilin 3.