Dissecting physical structure of calreticulin, an intrinsically disordered Ca2+ -buffering chaperone from endoplasmic reticulum

Journal of Biomolecular Structure & Dynamics
Anna Rita Migliaccio, V N Uversky

Abstract

Calreticulin (CALR) is a Ca2+ binding multifunctional protein that mostly resides in the endoplasmic reticulum (ER) and plays a number of important roles in various physiological and pathological processes. Although the major functions ascribed to CALR are controlling the Ca2+ homeostasis in ER and acting as a lectin-like ER chaperon for many glycoproteins, this moonlighting protein can be found in various cellular compartments where it has many non-ER functions. To shed more light on the mechanisms underlying polyfunctionality of this moonlighting protein that can be found in different cellular compartments and that possesses a wide spectrum of unrelated biological activities, being able to interact with Ca2+ (and potentially other metal ions), RNA, oligosaccharides, and numerous proteins, we used a set of experimental and computational tools to evaluate the intrinsic disorder status of CALR and the role of calcium binding on structural properties and conformational stability of the full-length CALR and its isolated P- and C-domains.

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Citations

Sep 3, 2020·Journal of Receptor and Signal Transduction Research·Biyong DengXin Chen
Dec 9, 2017·Frontiers in Cell and Developmental Biology·Lilian VarricchioAnna Rita Migliaccio
Jan 15, 2021·Platelets·Nora El JahraniAlexandre G de Brevern
Apr 4, 2021·International Journal of Molecular Sciences·Tanja Belčič MikičMatjaž Sever

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Methods Mentioned

BETA
NMR
X-ray
glycosylation
acetylation
ubiquitination

Software Mentioned

® VLXT
ESpritz
IUPred
STRING
DisEMBL
MobiDB
PONDR
JRONN
GlobPlot
MoRFpred

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