Abstract:
:Rab 11 GTPase is an important regulator of endocytic membrane traffic. Recently, we and others have identified a novel family of Rab11 binding proteins, known as Rab11-family interacting proteins (FIPs). One of the family members, Rab coupling protein (RCP), was identified as a protein binding to both Rab4 and Rab11 GTPases. RCP was therefore suggested to serve a dual function as Rab4 and Rab11 binding protein. In this study, we characterized the cellular functions of RCP and mapped its interactions with Rab4 and Rab11. Our data show that RCP interacts only weakly with Rab4 in vitro and does not play the role of coupling Rab11 and Rab4 in vivo. Furthermore, our data indicate that the RCP-Rab11 complex regulates the sorting of transferrin receptors from the degradative to the recycling pathway. We therefore propose that RCP functions primarily as a Rab11 binding protein that regulates protein sorting in tubular endosomes.
journal_name
Mol Biol Celljournal_title
Molecular biology of the cellauthors
Peden AA,Schonteich E,Chun J,Junutula JR,Scheller RH,Prekeris Rdoi
10.1091/mbc.e03-12-0918keywords:
subject
Has Abstractpub_date
2004-08-01 00:00:00pages
3530-41issue
8eissn
1059-1524issn
1939-4586pii
E03-12-0918journal_volume
15pub_type
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