Document Detail


A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum.
MedLine Citation:
PMID:  19597144     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Mammalian calreticulin (CRT) is a multifunctional Ca(2+)-binding protein involved in more than 40 cellular processes in various subcellular compartments, such as Ca(2+) storage and protein folding in the endoplasmic reticulum (ER). CRT homologues were discovered in plants almost 15 years ago, and recent studies revealed that many plant species contain 2 or more CRTs that are members of 2 distinct families, the CRT1/2 family and the plant-specific CRT3 family. However, little is known about their physiological functions. Here we report ebs2 (EMS-mutagenized bri1 suppressor 2) as an allele-specific suppressor of bri1-9, a dwarf Arabidopsis mutant caused by retention of a defective brassinosteroid receptor in the ER. EBS2 encodes the Arabidopsis CRT3 that interacts with ER-localized bri1-9 in a glycan-dependent manner. Loss-of-function ebs2 mutations compromise ER retention of bri1-9 and suppress its dwarfism, whereas EBS2 over-expression enhances its dwarf phenotype. In contrast, mutations of 2 other CRTs or their membrane-localized homologues calnexins had little effect on bri1-9. A domain-swapping experiment revealed that the positively charged C-terminal tail of CRT3 is crucial for its "bri1-9-retainer" function. Our study revealed not only a functional role for a plant-specific CRT, but also functional diversity among the 3 Arabidopsis CRT paralogues.
Authors:
Hua Jin; Zhi Hong; Wei Su; Jianming Li
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-07-13
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  106     ISSN:  1091-6490     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2009 Aug 
Date Detail:
Created Date:  2009-08-26     Completed Date:  2009-09-21     Revised Date:  2011-09-26    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13612-7     Citation Subset:  IM    
Affiliation:
Department of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.
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MeSH Terms
Descriptor/Qualifier:
Alleles
Amino Acid Sequence
Arabidopsis / genetics,  metabolism*
Arabidopsis Proteins / chemistry,  genetics,  metabolism*
Calreticulin / chemistry,  genetics,  metabolism*
Cholestanols / metabolism*
Cloning, Molecular
Endoplasmic Reticulum / metabolism*
Gene Expression Regulation, Plant
Genes, Plant
Molecular Sequence Data
Mutation / genetics
Phenotype
Plant Lectins / metabolism
Protein Binding
Receptors, Cell Surface / metabolism*
Species Specificity
Steroids, Heterocyclic / metabolism*
Suppression, Genetic
Grant Support
ID/Acronym/Agency:
R01 GM060519-08/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Calreticulin; 0/Cholestanols; 0/Plant Lectins; 0/Receptors, Cell Surface; 0/Steroids, Heterocyclic; 72962-43-7/brassinolide
Comments/Corrections
Comment In:
Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13151-2   [PMID:  19666569 ]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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