Open AccessInvolvement of a novel ADP‐ribosylation factor GTPase‐activating protein, SMAP, in membrane trafficking: Implications in cancer cell biology
Author(s) -
Tanabe Kenji,
Kon Shunsuke,
Natsume Waka,
Torii Tetsuo,
Watanabe Toshio,
Satake Masanobu
Publication year - 2006
Publication title -
cancer science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.035
H-Index - 141
eISSN - 1349-7006
pISSN - 1347-9032
DOI - 10.1111/j.1349-7006.2006.00251.x
Subject(s) - endocytosis , adp ribosylation factor , adherens junction , microbiology and biotechnology , biology , small gtpase , gtpase , cancer cell , gtpase activating protein , cadherin , cell , cancer , g protein , signal transduction , biochemistry , genetics , endoplasmic reticulum , golgi apparatus
The endocytosis of cell membrane proteins is initiated by the binding of activated Arf6, a member of Ras‐related GTPases, to the PM. A GAP specific for Arf6 triggers the budding of endocytotic vesicles from the PM by inactivating GTP‐bound Arf6. We recently identified the SMAP gene that encodes an ArfGAP and is involved in the endocytosis of TfnR and possibly E‐cadherin. In this review, we summarize the process of intracellular membrane trafficking, highlighting the roles played by the SMAP gene. Progression of cancer to malignancy occurs in parallel with the disappearance of E‐cadherin, a central component of the adherens junction in epithelial cells. Therefore, elucidation of the molecular mechanism of E‐cadherin endocytosis should be one of the key elements in tumor cell biology. ( Cancer Sci 2006; 97: 801–806)