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Rictor forms a complex with Cullin-1 to promote SGK1 ubiquitination and destruction.

Abstract：

:The Rictor/mTOR complex (also known as mTORC2) plays a critical role in cellular homeostasis by phosphorylating AGC kinases such as Akt and SGK at their hydrophobic motifs to activate downstream signaling. However, the regulation of mTORC2 and whether it has additional function(s) remain largely unknown. Here, we report that Rictor associates with Cullin-1 to form a functional E3 ubiquitin ligase. Rictor, but not Raptor or mTOR alone, promotes SGK1 ubiquitination. Loss of Rictor/Cullin-1-mediated ubiquitination leads to increased SGK1 protein levels as detected in Rictor null cells. Moreover, as part of a feedback mechanism, phosphorylation of Rictor at T1135 by multiple AGC kinases disrupts the interaction between Rictor and Cullin-1 to impair SGK1 ubiquitination. These findings indicate that the Rictor/Cullin-1 E3 ligase activity is regulated by a specific signal relay cascade and that misregulation of this mechanism may contribute to the frequent overexpression of SGK1 in various human cancers.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Gao D,Wan L,Inuzuka H,Berg AH,Tseng A,Zhai B,Shaik S,Bennett E,Tron AE,Gasser JA,Lau A,Gygi SP,Harper JW,DeCaprio JA,Toker A,Wei W

doi

10.1016/j.molcel.2010.08.016

subject

Has Abstract

pub_date

2010-09-10 00:00:00

pages

797-808

issue

5

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(10)00626-X

journal_volume

39

pub_type

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