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Title: Phosphorylation of RACK1 in plants

Receptor for Activated C Kinase 1 (RACK1) is a versatile scaffold protein that interacts with a large, diverse group of proteins to regulate various signaling cascades. RACK1 has been shown to regulate hormonal signaling, stress responses and multiple processes of growth and development in plants. However, little is known about the molecular mechanism underlying these regulations. Recently, it has been demonstrated that Arabidopsis RACK1 is phosphorylated by an atypical serine/threonine protein kinase, WITH NO LYSINE 8 (WNK8). Furthermore, RACK1 phosphorylation by WNK8 negatively regulates RACK1 function by influencing its protein stability. In conclusion, these findings promote a new regulatory system in which the action of RACK1 is controlled by phosphorylation and subsequent protein degradation.
Authors:
 [1]
  1. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Publication Date:
OSTI Identifier:
1265401
Grant/Contract Number:
AC05-00OR22725
Type:
Accepted Manuscript
Journal Name:
Plant Signaling & Behavior
Additional Journal Information:
Journal Volume: 10; Journal Issue: 8; Journal ID: ISSN 1559-2316
Publisher:
Taylor & Francis
Research Org:
Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Sponsoring Org:
USDOE Office of Science (SC); ORNL LDRD Seed-Money
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES arabidopsis; kinase; phosphorylation; protein degradation; RACK1; scaffold protein; WNK8