Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins
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ArticleKAUST Department
Biological and Environmental Science and Engineering (BESE) DivisionBioscience
Bioscience Program
Computational Bioscience Research Center (CBRC)
Environmental Science and Engineering Program
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
Structural Biology and Engineering
KAUST Grant Number
URF/1/4039-01Date
2021-05-14Online Publication Date
2021-05-14Print Publication Date
2021Submitted Date
2021-03-16Permanent link to this record
http://hdl.handle.net/10754/669443
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Show full item recordAbstract
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.Citation
Zhang, J., Vancea, A. I., Shahul Hameed, U. F., & Arold, S. T. (2021). Versatile control of the CDC48 segregase by the plant UBX-containing (PUX) proteins. Computational and Structural Biotechnology Journal, 19, 3125–3132. doi:10.1016/j.csbj.2021.05.025Sponsors
This research was supported by the King Abdullah University of Science and Technology (KAUST) through the baseline fund and the Award No. URF/1/4039-01 from the Office of Sponsored Research (OSR). We thank I. Blilou for comments on the manuscript.Publisher
Elsevier BVAdditional Links
https://linkinghub.elsevier.com/retrieve/pii/S2001037021002063ae974a485f413a2113503eed53cd6c53
10.1016/j.csbj.2021.05.025
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