An in vivo investigation of amino acid residues critical for the lectin function of arabidopsis calreticulin 3

Molecular Plant

Volumn 6, Issue 3, 2013, Pages 985-987

  Liu, Yidan ^a   Li, Jianming ^a  

^a UNIVERSITY OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS;

EID: 84875855045     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/sss163     Document Type: Letter

References (8)

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2. Jia, X.Y., He, L.H., Jiang, R.L., and Li, R.Z. (2009). Calreticulin: conserved protein and diverse functions in plants. Physiol. Plant. 136, 127-138.
3. Jin, H., Hong, Z., Su, W., and Li, J. (2009). A plant-specific calreticulin is a key retention factor for a defective brassinosteroid receptor in the endoplasmic reticulum. Proc. Natl Acad. Sci. U S A. 106, 13612-13617.
4. Jin, H., Yan, Z., Nam, K.H., and Li, J. (2007). Allele-specific suppression of a defective brassinosteroid receptor reveals a physiological role of UGGT in ER quality control. Mol. Cell. 26, 821-830.
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6. Michalak, M., Groenendyk, J., Szabo, E., Gold, L.I., and Opas, M. (2009). Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum. Biochem. J. 417, 651-666.
7. Schrag, J.D., Bergeron, J.J., Borisova, S., Hahn, M., Thomas, D.Y., and Cygler, M. (2001). The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell. 8, 633-644.
8. Thomson, S.P., and Williams, D.B. (2005). Delineation of the lectin site of the molecular chaperone calreticulin. Cell Stress Chaperones. 10, 242-251.