Related Experiment Video
Updated: May 29, 2026

Reconstitution of Msp1 Extraction Activity with Fully Purified Components
Published on: August 10, 2021
Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control
Hadas Peled-Zehavi1, Reut Yemini1, Nir Fluman1
1Department of Biomolecular Sciences, Weizmann Institute of Science, 234 Herzl St. PO Box 26, Rehovot 7610001, Israel.
Abstract:
Integral membrane proteins comprise at least a quarter of every proteome. To fold and function properly, these proteins must insert into the correct membrane with the proper topology and orientation. Although their transmembrane helices are chemically compatible with the bilayer, insertion inside cells is not a simple spontaneous event. It must occur in a crowded environment, at the correct membrane, and it often involves challenges such as transferring hydrophilic segments across the bilayer or accommodating helices that are only marginally compatible with it. Cells therefore rely on dedicated systems that direct membrane proteins to the membrane, mediate their insertion, and monitor the process to ensure that it occurs correctly. This review outlines the principles that govern membrane protein insertion in cells and explains how transmembrane sequence features interact with the machineries that mediate their entry into the bilayer. We highlight the major insertion systems of bacteria and eukaryotes and the auxiliary factors that support them, and describe how these pathways accommodate the broad range of membrane protein architectures found in cells, from single-pass proteins to complex multispanning transporters. We also discuss how cells maintain accuracy when insertion fails, through mechanisms that detect and resolve misinsertion. Together, these concepts present membrane protein insertion as a coordinated, adaptable, and safeguarded process, shaped by the interplay between sequence properties, membrane environments, and the machinery responsible for building the membrane proteome.
Related Concept Videos
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Insertion of Multi-pass Transmembrane Proteins in the RER
The multipass transmembrane proteins are the type IV integral membrane proteins with multiple topogenic sequences determining their spatial arrangement in the ER membrane. Nearly all multipass proteins lack a cleavable signal sequence and use...
Introduction to Membrane Traffic
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Introduction to Membrane Traffic
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Mitochondrial Protein Sorting
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Tail-anchoring of Proteins in the ER Membrane

