期刊
MOLECULAR BIOLOGY OF THE CELL
卷 17, 期 8, 页码 3625-3637出版社
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E05-08-0736
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资金
- NCI NIH HHS [P30 CA068485, CA-68485] Funding Source: Medline
- NICHD NIH HHS [P30 HD015052, HD15052] Funding Source: Medline
- NIDDK NIH HHS [DK-58404, DK-48370, R01 DK048370, R01 DK-51970, DK-43405, R01 DK051970, P60 DK020593, P30 DK020593, DK-20593, P30 DK058404, R01 DK043405] Funding Source: Medline
Rab11a, myosin Vb, and the Rab11-family interacting protein 2 (FIP2) regulate plasma membrane recycling in epithelial cells. This study sought to characterize more fully Rab11-FIP2 function by identifying kinase activities modifying Rab11-FIP2. We have found that gastric microsomal membrane extracts phosphorylate Rab11-FIP2 on serine 227. We identified the kinase that phosphorylated Rab11-FIP2 as MARK2/EMK1/Par-1B alpha (MARK2), and recombinant MARK2 phosphorylated Rab11-FIP2 only on serine 227. We created stable Madin-Darby canine kidney (MDCK) cell lines expressing enhanced green fluorescent protein-Rab11-FIP2 wild type or a nonphosphorylatable mutant [Rab11-FIP2(S227A)]. Analysis of these cell lines demonstrates a new role for Rab11-FIP2 in addition to that in the plasma membrane recycling system. In calcium switch assays, cells expressing Rab11-FIP2(S227A) showed a defect in the timely reestablishment of p120-containing junctional complexes. However, Rab11-FIP2(S227A) did not affect localization with recycling system components or the normal function of apical recycling and transcytosis pathways. These results indicate that phosphorylation of Rab11-FIP2 on serine 227 by MARK2 regulates an alternative pathway modulating the establishment of epithelial polarity.
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