Involvement of a novel ADP-ribosylation factor GTPase-activating protein, SMAP, in membrane trafficking: implications in cancer cell biology.

Abstract

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.

• Authors: Kenji Tanabe, Shunsuke Kon, Waka Natsume, Tetsuo Torii, Toshio Watanabe, Masanobu Satake
• Journal: Cancer science (Cancer Sci) Vol. 97 Issue 9 Pg. 801-6 (Sep 2006) ISSN: 1347-9032 [Print] England
• PMID: 16805823 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Review)

Chemical References

• Adaptor Proteins, Signal Transducing
• Cadherins
• Cytoskeletal Proteins
• KIFAP3 protein, human
• Receptors, Transferrin

Topics

• Adaptor Proteins, Signal Transducing (genetics, metabolism)
• Animals
• Cadherins (metabolism)
• Cell Membrane (metabolism)
• Cell Transformation, Neoplastic (metabolism)
• Cytoskeletal Proteins (genetics, metabolism)
• Endocytosis (physiology)
• Humans
• Protein Transport (physiology)
• Receptors, Transferrin (metabolism)
• Signal Transduction (physiology)