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A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum.

ABSTRACT: 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.

SUBMITTER: Jin H

PROVIDER: S-EPMC2726391 | biostudies-literature | 2009 Aug

REPOSITORIES: biostudies-literature

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A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum.

Jin Hua H Hong Zhi Z Su Wei W Li Jianming J

Proceedings of the National Academy of Sciences of the United States of America 20090713 32

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 ...[more]

PMID: 19597144

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Project description:BackgroundCalreticulin (CRT) is a chaperone protein, which aids correct folding of glycosylated proteins in the endoplasmic reticulum (ER). Under conditions of ER stress, CRT is upregulated and may be displayed on the surface of cells or be secreted. This 'ecto-CRT' may activate the innate immune response or it may aid clearance of apoptotic cells. Our and other studies have demonstrated upregulation of ER stress markers CHOP, BiP, ATF4, XBP1 and phosphorylated e-IF2 alpha (p-eIF2 alpha) in biopsy and post-mortem human multiple sclerosis (MS) samples. We extend this work by analysing changes in expression of CRT, BiP, CHOP, XBP1 and p-eIF2 alpha in a rat model of inflammatory demyelination. Demyelination was induced in the spinal cord by intradermal injection of recombinant mouse MOG mixed with incomplete Freund's adjuvant (IFA) at the base of the tail. Tissue samples were analysed by semi-quantitative scoring of immunohistochemically stained frozen tissue sections. Data generated following sampling of tissue from animals with spinal cord lesions, was compared to that obtained using tissue derived from IFA- or saline-injected controls. CRT present in rat serum and in a cohort of human serum derived from 14 multiple sclerosis patients and 11 healthy controls was measured by ELISA.ResultsStained tissue scores revealed significantly (p<0.05) increased amounts of CRT, CHOP and p-eIF2 alpha in the lesion, lesion edge and normal-appearing white matter when compared to controls. CHOP and p-eIF2 alpha were also significantly raised in regions of grey matter and the central canal (p<0.05). Immunofluorescent dual-label staining confirmed expression of these markers in astrocytes, microglia or neurons. Dual staining of rat and human spinal cord lesions with Oil Red O and CRT antibody showed co-localisation of CRT with the rim of myelin fragments. ELISA testing of sera from control and EAE rats demonstrated significant down-regulation (p<0.05) of CRT in the serum of EAE animals, compared to saline and IFA controls. This contrasted with significantly increased amounts of CRT detected in the sera of MS patients (p<0.05), compared to controls.ConclusionThis data highlights the potential importance of CRT and other ER stress proteins in inflammatory demyelination.

Dataset Information

A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum.

Publications

A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum.

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