Crowding Effects of Membrane Proteins

被引：44

作者：

Zhou, Huan-Xiang ^{[1
,2
]}

机构：

[1] Florida State Univ, Dept Phys, Tallahassee, FL 32306 USA

[2] Florida State Univ, Inst Mol Biophys, Tallahassee, FL 32306 USA

来源：

JOURNAL OF PHYSICAL CHEMISTRY B | 2009年 / 113卷 / 23期

关键词：

LOCALLY PLANAR SURFACES; LIPID RAFTS; GLOBULAR-PROTEINS; ADSORPTION; AGGREGATION; BINDING; AREA; SIMULATIONS; EQUILIBRIA; OCCUPANCY;

D O I：

10.1021/jp8107446

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

In cell membranes, membrane proteins occupy similar to 30% of the total surface area. Crowding effects similar to those in the solution phase are thus to be expected. In addition, there are crowding effects unique to proteins bound to the two-dimensional membranes, such as those exerted on the equilibration of a protein between two membrane orientations and on the redistribution of proteins between different locations in a cell membrane. This article aims to present a theoretical framework for understanding the various crowding effects within membranes. For illustration, the theory is used to analyze previously published experimental and simulation data. It is hoped that the article will encourage quantitative analyses in future experiments and spur systematic investigation of membrane crowding effects.

引用

页码：7995 / 8005

页数：11

共 39 条

[1] Macromolecular crowding at membrane interfaces:: Adsorption and alignment of membrane peptides [J].

Aisenbrey, Christopher ;

Bechinger, Burkhard ;

Groebner, Gerhard .

JOURNAL OF MOLECULAR BIOLOGY, 2008, 375 (02) :376-385

[2]

Alberts B., 2007, Molecular Biology of the Cell. (4th edition), Vfifth

[3] Structure of α-helical membrane-bound human islet amyloid polypeptide and its implications for membrane-mediated misfolding [J].

Apostolidou, Melania ;

Jayasinghe, Sajith A. ;

Langen, Ralf .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (25) :17205-17210

[4] Two types of Alzheimer's β-amyloid (1-40) peptide membrane interactions:: Aggregation preventing transmembrane anchoring Versus accelerated surface fibril formation [J].

Bokvist, M ;

Lindström, F ;

Watts, A ;

Gröbner, G .

JOURNAL OF MOLECULAR BIOLOGY, 2004, 335 (04) :1039-1049

[5] Misfolding of amyloidogenic proteins at membrane surfaces:: The impact of macromolecular crowding [J].

Bokvist, Marcus ;

Grobner, Gerhard .

JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2007, 129 (48) :14848-+

[6] Adsorption of globular proteins on locally planar surfaces: Models for the effect of excluded surface area and aggregation of adsorbed protein on adsorption equilibria [J].

Chatelier, RC ;

Minton, AP .

BIOPHYSICAL JOURNAL, 1996, 71 (05) :2367-2374

[7] Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions [J].

Cunningham, O ;

Andolfo, A ;

Santovito, ML ;

Iuzzolino, L ;

Blasi, F ;

Sidenius, N .

EMBO JOURNAL, 2003, 22 (22) :5994-6003

[8] Mesoscopic Monte Carlo simulations of stochastic encounters between photoactivated rhodopsin and transducin in disc membranes [J].

Dell'Orco, Daniele ;

Schmidt, Henning .

JOURNAL OF PHYSICAL CHEMISTRY B, 2008, 112 (14) :4419-4426

[9] Protein area occupancy at the center of the red blood cell membrane [J].

Dupuy, Allison D. ;

Engelman, Donald M. .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2008, 105 (08) :2848-2852

[10] Differential sorting and fate of endocytosed GPI-anchored proteins [J].

Fivaz, M ;

Vilbois, F ;

Thurnheer, S ;

Pasquali, C ;

Abrami, L ;

Bickel, PE ;

Parton, RG ;

van der Goot, FG .

EMBO JOURNAL, 2002, 21 (15) :3989-4000

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