Complement C1q Binding Protein (C1QBP): Physiological Functions, Mutation-Associated Mitochondrial Cardiomyopathy and Current Disease Models

Jie Wang,Christopher L-H Huang,Yanmin Zhang

doi:10.3389/fcvm.2022.843853

Abstract

Complement C1q binding protein (C1QBP, p32) is primarily localized in mitochondrial matrix and associated with mitochondrial oxidative phosphorylative function. C1QBP deficiency presents as a mitochondrial disorder involving multiple organ systems. Recently, disease associated C1QBP mutations have been identified in patients with a combined oxidative phosphorylation deficiency taking an autosomal recessive inherited pattern. The clinical spectrum ranges from intrauterine growth restriction to childhood (cardio) myopathy and late-onset progressive external ophthalmoplegia. This review summarizes the physiological functions of C1QBP, its mutation-associated mitochondrial cardiomyopathy shown in the reported available patients and current experimental disease platforms modeling these conditions.

Highlights

Mitochondrial diseases form a diverse group of heritable disorders caused by a wide spectrum of mutations in nuclear or mitochondrial genes [1, 2]
This review summarizes the physiological functions of C1q Binding Protein (C1QBP), its mutation-associated mitochondrial cardiomyopathy shown in the reported available patients and current experimental disease platforms modeling these conditions
This review summarizes physiological functions of C1QBP, its mutation-associated mitochondrial cardiomyopathy, and current disease models

Summary

Introduction

Mitochondrial diseases form a diverse group of heritable disorders caused by a wide spectrum of mutations in nuclear or mitochondrial genes [1, 2]. Complement C1q Binding Protein (C1QBP): Physiological Functions, Mutation-Associated Mitochondrial Cardiomyopathy and Current Disease Models This review summarizes the physiological functions of C1QBP, its mutation-associated mitochondrial cardiomyopathy shown in the reported available patients and current experimental disease platforms modeling these conditions. This review summarizes physiological functions of C1QBP, its mutation-associated mitochondrial cardiomyopathy, and current disease models.

Results

Conclusion