Calnexin is a chaperone, characterized by assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. It specifically acts to retain unfolded or unassembled N-linked glycoproteins in the ER.

Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone ...

In this chapter we present the evidence that calnexin (CNX) and calreticulin (CRT) function as molecular chaperones to assist in the folding and subunit assembly of the majority of Asn-linked glycoproteins that pass through the endoplasmic reticulum.

2023年1月24日 · Calnexin is a type I integral endoplasmic reticulum (ER) membrane protein with an N-terminal domain that resides in the lumen of the ER and a C-terminal domain that extends into the cytosol. Calnexin is commonly referred to as a molecular chaperone involved in the folding and quality control of memb …

2024年12月24日 · This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked …

Calreticulin and calnexin are Ca2+-binding proteins with chaperone activity in the endoplasmic reticulum. These proteins have been eliminated by gene replacement in Dictyostelium, the only microorganism known to harbor both proteins; family members ...

Calnexin is a new type of molecular chaperone that interacts with many nascent membrane and soluble proteins of the secretory pathway. Calnexin is unrelated to molecular chaperones of the Hsp60, Hsp70 and Hsp90 families, and is further distinguished from them in that it is an integral membrane prote …

2006年1月19日 · Here, we investigate whether calnexin functions as a chaperone for Rh1 and whether mutations in calnexin lead to neurodegeneration. In addition to its role as a molecular chaperone, calnexin is thought to bind Ca 2+ at two distinct sites.

Calnexin, a single-pass membrane protein, and calreticulin, a soluble protein, are lectins (sugar-binding proteins) that bind to N-linked oligosaccharides containing a single glucose residue. From: Goodman's Medical Cell Biology (Fourth Edition), 2021

Gutiérrez et al. investigated the role of calnexin, an ER chaperone that interacts with SERCA, the ATPase that pumps Ca 2+ into the ER, in mitochondrial bioenergetics. The authors found that calnexin maintained SERCA in a redox state that was optimal for activity.