4.7 Review

Multifaceted roles of HEAT SHOCK PROTEIN 90 molecular chaperones in plant development

Journal

JOURNAL OF EXPERIMENTAL BOTANY
Volume 71, Issue 14, Pages 3966-3985

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/jxb/eraa177

Keywords

Chaperone; client protein; co-chaperone; HEAT SHOCK PROTEIN 90; plant cell; plant development; protein kinase

Categories

Funding

  1. Grantova Agentura Ceske Republiky GACR [17-24500S]
  2. European Regional Development Fund project Plants as a tool for sustainable global development [CZ.02.1.01/0.0/0.0/16_ 019/0000827]

Ask authors/readers for more resources

HEAT SHOCK PROTEINS 90 (HSP90s) are molecular chaperones that mediate correct folding and stability of many client proteins. These chaperones act as master molecular hubs involved in multiple aspects of cellular and developmental signalling in diverse organisms. Moreover, environmental and genetic perturbations affect both HSP9Os and their clients, leading to alterations of molecular networks determining respectively plant phenotypes and genotypes and contributing to a broad phenotypic plasticity. Although HSP90 interaction networks affecting the genetic basis of phenotypic variation and diversity have been thoroughly studied in animals, such studies are just starting to emerge in plants. Here, we summarize current knowledge and discuss HSP90 network functions in plant development and cellular homeostasis.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available