Abstract：
:The Rab11 family of small GTPases is composed of three members, Rab11a, Rab11b, and Rab25. While recent work on Rab11a and Rab25 has yielded some insights into their function, Rab11b has received little attention. Therefore, we sought to examine the distribution of endogenous Rab11b in epithelial cells. In rabbit gastric parietal cells, unlike Rab11a, Rab11b did not colocalize or coisolate with H(+)/K(+)-ATPase. In MDCK cells, endogenous Rab11b localized to an apical pericentrisomal region distinct from Rab11a. The microtubule agents nocodazole and taxol dramatically alter Rab11a's localization in the cell, while effects on Rab11b's distribution were less apparent. These results indicate that in contrast to Rab11a, the Rab11b compartment in the apical region is not as dependent upon microtubules. While Rab11a is known to regulate transferrin trafficking in nonpolarized cells and IgA trafficking in polarized cells, Rab11b exhibited little colocalization with either of these cargoes. Thus, while Rab11a and Rab11b share high sequence homology, they appear to reside within distinct vesicle compartments.
journal_name
Exp Cell Resjournal_title
Experimental cell researchauthors
Lapierre LA,Dorn MC,Zimmerman CF,Navarre J,Burnette JO,Goldenring JRdoi
10.1016/s0014-4827(03)00340-9keywords:
subject
Has Abstractpub_date
2003-11-01 00:00:00pages
322-31issue
2eissn
0014-4827issn
1090-2422pii
S0014482703003409journal_volume
290pub_type
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