2010 Fiscal Year Final Research Report
Role of Rab13 binding protein JRAB/MICAL-L2 in regulating cell polarity and adhesion
Project/Area Number |
20590283
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
General medical chemistry
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Research Institution | The University of Tokushima |
Principal Investigator |
NISHIMURA Noriyuki The University of Tokushima, 大学院・医学研究科, 准教授 (00322719)
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Project Period (FY) |
2008 – 2010
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Keywords | JRAB / MICAL-L2 / Rab13 / Rab8 / アクチニン4 / タイトジャンクション / アドヘレンスジャンクション |
Research Abstract |
Dynamic rearrangement of epithelial cell junctions, tight junction (TJ) and adherens junction (AJ), is essential to maintain the homeostasis of the organism in response to various stimuli. The transport of integral TJ and AJ proteins, claudins, occludins and cadherins, to and/or from the plasma membrane enables this rearrangement. We previously revealed that Rab13 and JRAB/MICAL-L2 (JRAB) mediated the endocytic recycling of occludin. In the present study, we identified Rab8 and actinin-4 as JRAB-binding proteins by using yeast two-hybrid screening. Rab13 and Rab8 competed with each other for the binding to JRAB and functionally associated with JRAB at the plasma membrane and recycling endosome, respectively. Furthermore, Rab13-bound JRAB was targeted to the plasma membrane through its binding to actinin-4. These results suggest that JRAB regulates epithelial cell polarity and adhesion through its binding to Rab13, Rab8 and actinin-4.
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[Journal Article] Rab15 expression correlates with retinoic acid-induced differentiation of neuroblastoma cells.2011
Author(s)
Nishimura N, Pham TVH, Hartomo TB, Lee MJ, Hasegawa D, Takeda H, Kawasaki K, Kosaka Y, Yamamoto T, Morikawa S, Yamamoto N, Kubokawa I, Mori T, Yanai T, Hayakawa A, Takeshima Y, Nishio H, Matsuo M.
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Journal Title
Oncol.Rep. 26
Pages: 145-151
Peer Reviewed
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