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

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, oligos

SUBMITTER: Migliaccio AR 

PROVIDER: S-EPMC6243143 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature