Cullin-associated NEDD8-dissociated protein 1

Definition:

Key assembly factor of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complexes that promotes the exchange of the substrate-recognition F-box subunit in SCF complexes, thereby playing a key role in the cellular repertoire of SCF complexes. Acts as a F-box protein exchange factor. The exchange activity of CAND1 is coupled with cycles of neddylation conjugation: in the deneddylated state, cullin-binding CAND1 binds CUL1-RBX1, increasing dissociation of the SCF complex and promoting exchange of the F-box protein. Probably plays a similar role in other cullin-RING E3 ubiquitin ligase complexes.

References:

[1]. Yee Shin Chua, et al. Regulation of cullin RING E3 ubiquitin ligases by CAND1 in vivo. PLoS One. 2011 Jan 13;6(1):e16071. [Content Brief]

[2]. Kyoeng-Woo Min, et al. TIP120A associates with cullins and modulates ubiquitin ligase activity. J Biol Chem. 2003 May 2;278(18):15905-10. [Content Brief]

[3]. Nathan W Pierce, et al. Cand1 promotes assembly of new SCF complexes through dynamic exchange of F box proteins. Cell. 2013 Mar 28;153(1):206-15. [Content Brief]

[4]. Jianyu Zheng, et al. CAND1 binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex. Mol Cell. 2002 Dec;10(6):1519-26. [Content Brief]

[5]. Jidong Liu, et al. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol Cell. 2002 Dec;10(6):1511-8. [Content Brief]

[6]. Shih-Ching Lo, et al. CAND1-mediated substrate adaptor recycling is required for efficient repression of Nrf2 by Keap1. Mol Cell Biol. 2006 Feb;26(4):1235-44. [Content Brief]

Biomedical Dictionary

The Biomedical Dictionary is a comprehensive and professional collection of biological academic terms and subject datas. All explanations are supported by authoritative books or high impact factor literatures, and you can acquire accurate explanations of the biomedical terms you want to know.

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z #

Name
Email *

	Sorry, but the email address you supplied was invalid.