Probing the Molecular Basis of SUMO-Mediated Signaling Pathway by NMR

doi:10.11938/cjmr20150203

Abstract

Abstract:

Post-translational modification by Small Ubiquitin-like MOdifier (SUMO) proteins regulates a diverse array of cellular events. The signaling process is initiated by attaching SUMO to the E1 activating protein. In the second step SUMO is transferred to E2 conjugating protein (Ubc9). Lastly, Ubc9 couples SUMO to a target substrate covalently. The process is terminated by protease removal of SUMOs from the substrates. Sumoylation is regulated primarily through specific recognition of the sumoylation motif (SM) by Ubc9 and, in some cases, by E3-substrate recognition. The functional consequences of SUMO modification are mostly mediated by recruitment of effector proteins that contain a SUMO Interaction Motif (SIM). Furthermore, SUMO can form poly-SUMO conjugate, which can be recognized by proteins containing poly-SIMs, such as the RING-finger 4 (RNF4) ubiquitin E3 ligase. RNF4 contains four SIMs that
facilitate poly-SUMO-specific ubiquitination and targets poly-sumoylated proteins for degradation. Here we review NMR structure-functional studies, conducted in our laboratory and aimed at dissecting the molecular basis of SUMO-mediated pathway.

Key words: liquid NMR, structure, SUMO, PML, Daxx, RNF4

CLC Number:

O482.53

HUANG Tai-huang. Probing the Molecular Basis of SUMO-Mediated Signaling Pathway by NMR[J]. Chinese Journal of Magnetic Resonance, 2015, 32(2): 163-180.

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