The Ball and Chain of Polyubiquitin Structures

TY - JOUR

T1 - The Ball and Chain of Polyubiquitin Structures

AU - Alfano, Caterina

AU - Faggiano, Serena

AU - Pastore, Annalisa

PY - 2016/4

Y1 - 2016/4

N2 - Ubiquitylation is a post-translational modification implicated in several different cellular pathways. The possibility of forming chains through covalent crosslinking between any of the seven lysines, or the initial methionine, and the C terminus of another moiety provides ubiquitin (Ub) with special flexibility in its function in signalling. Here, we review the knowledge accumulated over the past several years about the functions and structural features of polyUb chains. This analysis reveals the need to understand further the functional role of some of the linkages and the structural code that determines recognition of polyUbs by protein partners.

AB - Ubiquitylation is a post-translational modification implicated in several different cellular pathways. The possibility of forming chains through covalent crosslinking between any of the seven lysines, or the initial methionine, and the C terminus of another moiety provides ubiquitin (Ub) with special flexibility in its function in signalling. Here, we review the knowledge accumulated over the past several years about the functions and structural features of polyUb chains. This analysis reveals the need to understand further the functional role of some of the linkages and the structural code that determines recognition of polyUbs by protein partners.

KW - biophysics

KW - post-translational modifications

KW - proteasomal pathway

KW - signalling

KW - structure

KW - ubiquitin

U2 - 10.1016/j.tibs.2016.01.006

DO - 10.1016/j.tibs.2016.01.006

M3 - Article

SN - 0968-0004

VL - 41

SP - 371

EP - 385

JO - TRENDS IN BIOCHEMICAL SCIENCES

JF - TRENDS IN BIOCHEMICAL SCIENCES

IS - 4

ER -