TM4SF5-mediated protein-protein networks and tumorigenic roles

Transmembrane 4 L six family member 5 (TM4SF5), as a membrane glycoprotein with 4 transmembrane domains, is similar to the tetraspanins in terms of membrane topology and plays important roles in tumorigenesis and tumor metastasis. Especially, TM4SF5 appears to form a massive protein-protein complex...

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Bibliographic Details
Published inBMB reports Vol. 47; no. 9; pp. 483 - 487
Main Author Lee, Jung Weon
Format Journal Article
LanguageKorean
Published 2014
Subjects
Fibrosis
Cytokine receptors
TM4SF5
Metastasis
EGFR
Integrins
Tetraspanin
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Summary:Transmembrane 4 L six family member 5 (TM4SF5), as a membrane glycoprotein with 4 transmembrane domains, is similar to the tetraspanins in terms of membrane topology and plays important roles in tumorigenesis and tumor metastasis. Especially, TM4SF5 appears to form a massive protein-protein complex consisting of diverse membrane proteins and/or receptors in addition to cytosolic signaling molecules to regulate their signaling activities during the pathological processes. TM4SF5 is shown to interact with integrins ${\alpha}2$, ${\alpha}5$, and ${\beta}1$, EGFR, IL6R, CD151, focal adhesion kinase (FAK), and c-Src. This review focuses on the significance of the interactions with regards to TM4SF5-positive tumorigenesis and metastasis.
Bibliography:KISTI1.1003/JNL.JAKO201429339406715
ISSN:1976-6696
1976-670X