Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum.
Calreticulin is a ubiquitous endoplasmic reticulum Ca2+ binding chaperone. The protein has been implicated in a variety of diverse functions. Calreticulin is a lectin-like chaperone and, together with calnexin, it plays an important role in quality control during protein synthesis, folding, and posttranslational modification. Calreticulin binds Ca2+ and affects cellular Ca2+ homeostasis. The protein increases the Ca2+ storage capacity of the endoplasmic reticulum and modulates the function of endoplasmic reticulum Ca2+-ATPase. Calreticulin also plays a role in the control of cell adhesion and steroid-sensitive gene expression. Recently, the protein has been identified and characterized in higher plants but its precise role in plant cells awaits further investigation.
Michalak
M
M
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Mariani
P
P
Opas
M
M
D000818:Animals; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000502:physiology*; D037282:Calreticulin; D002448:Cell Adhesion; D004721:Endoplasmic Reticulum / Q000737:chemistry*; D017343:Genes, Plant; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D008954:Models, Biological; D018832:Molecular Chaperones / Q000737:chemistry*; D010802:Phylogeny; D012261:Ribonucleoproteins / Q000737:chemistry* / Q000502:physiology*
D002135:Calcium-Binding Proteins; D037282:Calreticulin; D018832:Molecular Chaperones; D012261:Ribonucleoproteins