The complexities of p97 function in health and disease

Eli Chapman, Anastasia N. Fry, Minjin Kang

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

p97 is a homohexameric, toroidal machine that harnesses the energy of ATP binding and hydrolysis to effect structural reorganization of a diverse and primarily uncharacterized set of substrate proteins. This action has been linked to endoplasmic reticulum associated degradation (ERAD), homotypic membrane fusion, transcription factor control, cell cycle progression, DNA repair, and post-mitotic spindle disassembly. Exactly how these diverse processes use p97 is not fully understood, but it is clear that binding sites, primarily on the N-and C-domains of p97, facilitate this diversity by coordinating a growing collection of cofactors. These cofactors act at the levels of mechanism, sub-cellular localization, and substrate modification. Another unifying theme is the use of ubiquitylation. Both p97 and many of the associated cofactors have demonstrable ubiquitin-binding competence. The present review will discuss some of the current mechanistic studies and controversies and how these relate to cofactors as well as discussing potential therapeutic targeting of p97.

Original languageEnglish (US)
Pages (from-to)700-710
Number of pages11
JournalMolecular BioSystems
Volume7
Issue number3
DOIs
StatePublished - Mar 1 2011
Externally publishedYes

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Endoplasmic Reticulum-Associated Degradation
Spindle Apparatus
Membrane Fusion
Ubiquitination
Ubiquitin
Cell Cycle Checkpoints
DNA Repair
Mental Competency
Hydrolysis
Transcription Factors
Adenosine Triphosphate
Binding Sites
Health
Proteins
Therapeutics

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology

Cite this

The complexities of p97 function in health and disease. / Chapman, Eli; Fry, Anastasia N.; Kang, Minjin.

In: Molecular BioSystems, Vol. 7, No. 3, 01.03.2011, p. 700-710.

Research output: Contribution to journalArticle

Chapman, Eli ; Fry, Anastasia N. ; Kang, Minjin. / The complexities of p97 function in health and disease. In: Molecular BioSystems. 2011 ; Vol. 7, No. 3. pp. 700-710.
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