Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins

Junrui Zhang; Alexandra I Vancea; Umar F Shahul Hameed; Stefan T Arold

doi:10.1016/j.csbj.2021.05.025

Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins

Comput Struct Biotechnol J. 2021 May 14:19:3125-3132. doi: 10.1016/j.csbj.2021.05.025. eCollection 2021.

Authors

Junrui Zhang¹, Alexandra I Vancea¹, Umar F Shahul Hameed¹, Stefan T Arold^{1

2}

Affiliations

¹ King Abdullah University of Science and Technology (KAUST), Computational Bioscience Research Center (CBRC), Biological and Environmental Science and Engineering (BESE), Thuwal 23955-6900, Saudi Arabia.
² Centre de Biochimie Structurale, CNRS, INSERM, Université de Montpellier, 34090 Montpellier, France.

Abstract

In plants, AAA-adenosine triphosphatase (ATPase) Cell Division Control Protein 48 (CDC48) uses the force generated through ATP hydrolysis to pull, extract, and unfold ubiquitylated or sumoylated proteins from the membrane, chromatin, or protein complexes. The resulting changes in protein or RNA content are an important means for plants to control protein homeostasis and thereby adapt to shifting environmental conditions. The activity and targeting of CDC48 are controlled by adaptor proteins, of which the plant ubiquitin regulatory X (UBX) domain-containing (PUX) proteins constitute the largest family. Emerging knowledge on the structure and function of PUX proteins highlights that these proteins are versatile factors for plant homeostasis and adaptation that might inspire biotechnological applications.

Keywords: Adaptor; Autophagy; CDC48; Cofactors; ERAD; LDAD; PUX proteins; Segregase; Structure.

Publication types

Review