NDLI: Mechanisms of integral membrane protein insertion and folding

Content Provider	PubMed Central
Author	Florian, Cymer Heijne, Gunnar Von White, Stephen H.
Copyright Year	2014
Abstract	The biogenesis, folding, and structure of α-helical membrane proteins (MPs) are important to understand because they underlie virtually all physiological processes in cells including key metabolic pathways, such as the respiratory chain and the photosystems, and the transport of solutes and signals across membranes. Nearly all MPs require translocons—often referred to as protein-conducting channels—for proper insertion into their target membrane. Remarkable progress toward understanding the structure and functioning of translocons has been made during the past decade. Here we review and assess this progress critically. All available evidence indicates that MPs are equilibrium structures that achieve their final structural states by folding along thermodynamically controlled pathways. The main challenge for cells is the targeting and membrane insertion of highly hydrophobic amino acid sequences. Targeting and insertion are managed in cells principally by interactions between ribosomes and membrane-embedded translocons. Our review examines the biophysical and biological boundaries of membrane protein insertion and the folding of polytopic membrane proteins in vivo. A theme of the review is the under-appreciated role of basic thermodynamic principles in MP folding and assembly. Thermodynamics not only dictates the final folded structure, it is the driving force for the evolution of the ribosome-translocon system of assembly. We conclude the review with a perspective suggesting a new view of translocon-guided MP insertion.
Related Links	http://dx.doi.org/10.1016/j.jmb.2014.09.014
Ending Page	1022
Page Count	24
Starting Page	999
File Format	PDF
ISSN	00222836
e-ISSN	10898638
Journal	Journal of molecular biology
Issue Number	5
Volume Number	427
Language	English
Publisher Date	2015-03-01
Access Restriction	Open
Subject Keyword	Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology Biophysics

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Cellular Mechanisms of Membrane Protein Folding

Mechanisms of Integral Membrane Protein Insertion and Folding

Fast kinetics and mechanisms in protein folding.

SecA Drives Transmembrane Insertion of RodZ, an Unusual Single-Span Membrane Protein

Structural and Functional Dynamics of an Integral Membrane Protein Complex Modulated by Lipid Headgroup Charge

MECHANISM AND HYDROPHOBIC FORCES DRIVING MEMBRANE PROTEIN INSERTION OF SUBUNIT II OF CYTOCHROME BO OXIDASE

Malleability of the Folding Mechanism of the Outer Membrane Protein PagP: Parallel Pathways and the Effect of Membrane Elasticity

Modulating bilayer mechanical properties to promote the coupled folding and insertion of an integral membrane protein

Folding and Insertion of Transmembrane Helices at the ER

Mechanisms of integral membrane protein insertion and folding

Similar Documents

Cellular Mechanisms of Membrane Protein Folding

Mechanisms of Integral Membrane Protein Insertion and Folding

Fast kinetics and mechanisms in protein folding.

SecA Drives Transmembrane Insertion of RodZ, an Unusual Single-Span Membrane Protein

Structural and Functional Dynamics of an Integral Membrane Protein Complex Modulated by Lipid Headgroup Charge

MECHANISM AND HYDROPHOBIC FORCES DRIVING MEMBRANE PROTEIN INSERTION OF SUBUNIT II OF CYTOCHROME BO OXIDASE

Malleability of the Folding Mechanism of the Outer Membrane Protein PagP: Parallel Pathways and the Effect of Membrane Elasticity

Modulating bilayer mechanical properties to promote the coupled folding and insertion of an integral membrane protein

Folding and Insertion of Transmembrane Helices at the ER

Mechanisms of integral membrane protein insertion and folding