DCN1-like protein 1

Definition:

Part of an E3 ubiquitin ligase complex for neddylation. Promotes neddylation of cullin components of E3 cullin-RING ubiquitin ligase complexes. Acts by binding to cullin-RBX1 complexes in the cytoplasm and promoting their nuclear translocation, enhancing recruitment of E2-NEDD8 (UBE2M-NEDD8) thioester to the complex, and optimizing the orientation of proteins in the complex to allow efficient transfer of NEDD8 from the E2 to the cullin substrates. Involved in the release of inhibitory effets of CAND1 on cullin-RING ligase E3 complex assembly and activity. Acts also as an oncogene facilitating malignant transformation and carcinogenic progression (By similarity).

References:

[1]. Matthew J Keuss, et al. Characterization of the mammalian family of DCN-type NEDD8 E3 ligases. J Cell Sci. 2016 Apr 1;129(7):1441-54. [Content Brief]

[2]. Pardeep Heir, et al. DCNL1 functions as a substrate sensor and activator of cullin 2-RING ligase. Mol Cell Biol. 2013 Apr;33(8):1621-31. [Content Brief]

[3]. Alexander Y Kim, et al. SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation. J Biol Chem. 2008 Nov 28;283(48):33211-20. [Content Brief]

[4]. Daniel C Scott, et al. Blocking an N-terminal acetylation-dependent protein interaction inhibits an E3 ligase. Nat Chem Biol. 2017 Aug;13(8):850-857. [Content Brief]

[5]. Guochang Huang, et al. SCCRO3 (DCUN1D3) antagonizes the neddylation and oncogenic activity of SCCRO (DCUN1D1). J Biol Chem. 2014 Dec 12;289(50):34728-42. [Content Brief]

[6]. Nathalie Meyer-Schaller, et al. The human Dcn1-like protein DCNL3 promotes Cul3 neddylation at membranes. Proc Natl Acad Sci U S A. 2009 Jul 28;106(30):12365-70. [Content Brief]

[7]. Julie K Monda, et al. Structural conservation of distinctive N-terminal acetylation-dependent interactions across a family of mammalian NEDD8 ligation enzymes. Structure. 2013 Jan 8;21(1):42-53. [Content Brief]

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