Calreticulin: one protein, one gene, many functions. Review uri icon

Overview

abstract

  • The endoplasmic reticulum (ER) plays a critical role in the synthesis and chaperoning of membrane-associated and secreted proteins. The membrane is also an important site of Ca(2+) storage and release. Calreticulin is a unique ER luminal resident protein. The protein affects many cellular functions, both in the ER lumen and outside of the ER environment. In the ER lumen, calreticulin performs two major functions: chaperoning and regulation of Ca(2+) homoeostasis. Calreticulin is a highly versatile lectin-like chaperone, and it participates during the synthesis of a variety of molecules, including ion channels, surface receptors, integrins and transporters. The protein also affects intracellular Ca(2+) homoeostasis by modulation of ER Ca(2+) storage and transport. Studies on the cell biology of calreticulin revealed that the ER membrane is a very dynamic intracellular compartment affecting many aspects of cell physiology.

publication date

  • December 1, 1999

Research

keywords

  • Calcium
  • Calcium-Binding Proteins
  • Endoplasmic Reticulum
  • Lectins
  • Molecular Chaperones
  • Ribonucleoproteins

Identity

PubMed Central ID

  • PMC1220642

Scopus Document Identifier

  • 0033460216

PubMed ID

  • 10567207

Additional Document Info

volume

  • 344 Pt 2

issue

  • Pt 2