Weak dependence of mobility of membrane protein aggregates on aggregate size supports a viscous model of retardation of diffusion

Dennis F. Kucik, Elliot L. Elson, Michael Sheetz

Research output: Contribution to journalArticle

61 Citations (Scopus)

Abstract

Proteins in plasma membranes diffuse more slowly than proteins inserted into artificial lipid bilayers. On a long-range scale (>250 nm), submembrane barriers, or skeleton fences that hinder long-range diffusion and create confinement zones, have been described. Even within such confinement zones, however, diffusion of proteins is much slower than predicted by the viscosity of the lipid. The cause of this slowing of diffusion on the micro scale has not been determined and is the focus of this paper. One way to approach this question is to determine the dependence of particle motion on particle size. Some current models predict that the diffusion coefficient of a membrane protein aggregate will depend strongly on its size, while others do not. We have measured the diffusion coefficients of membrane glycoprotein aggregates linked together by concanavalin A molecules bound to beads of various sizes, and also the diffusion coefficients of individual concanavalin A binding proteins. The measurements demonstrate at most a weak dependence of diffusion coefficient on aggregate size. This finding supports retardation by viscous effects, and is not consistent with models involving direct interaction of diffusing proteins with cytoskeletal elements.

Original languageEnglish (US)
Pages (from-to)314-322
Number of pages9
JournalBiophysical Journal
Volume76
Issue number1 I
DOIs
StatePublished - Jan 1 1999
Externally publishedYes

Fingerprint

Membrane Proteins
Concanavalin A
Proteins
Cytoskeletal Proteins
Membrane Glycoproteins
Lipid Bilayers
Protein Aggregates
Particle Size
Skeleton
Viscosity
Carrier Proteins
Cell Membrane
Lipids

ASJC Scopus subject areas

  • Biophysics

Cite this

Weak dependence of mobility of membrane protein aggregates on aggregate size supports a viscous model of retardation of diffusion. / Kucik, Dennis F.; Elson, Elliot L.; Sheetz, Michael.

In: Biophysical Journal, Vol. 76, No. 1 I, 01.01.1999, p. 314-322.

Research output: Contribution to journalArticle

@article{a5a0c481d1f64576aaf7917f9194fa82,
title = "Weak dependence of mobility of membrane protein aggregates on aggregate size supports a viscous model of retardation of diffusion",
abstract = "Proteins in plasma membranes diffuse more slowly than proteins inserted into artificial lipid bilayers. On a long-range scale (>250 nm), submembrane barriers, or skeleton fences that hinder long-range diffusion and create confinement zones, have been described. Even within such confinement zones, however, diffusion of proteins is much slower than predicted by the viscosity of the lipid. The cause of this slowing of diffusion on the micro scale has not been determined and is the focus of this paper. One way to approach this question is to determine the dependence of particle motion on particle size. Some current models predict that the diffusion coefficient of a membrane protein aggregate will depend strongly on its size, while others do not. We have measured the diffusion coefficients of membrane glycoprotein aggregates linked together by concanavalin A molecules bound to beads of various sizes, and also the diffusion coefficients of individual concanavalin A binding proteins. The measurements demonstrate at most a weak dependence of diffusion coefficient on aggregate size. This finding supports retardation by viscous effects, and is not consistent with models involving direct interaction of diffusing proteins with cytoskeletal elements.",
author = "Kucik, {Dennis F.} and Elson, {Elliot L.} and Michael Sheetz",
year = "1999",
month = "1",
day = "1",
doi = "10.1016/S0006-3495(99)77198-5",
language = "English (US)",
volume = "76",
pages = "314--322",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "1 I",

}

TY - JOUR

T1 - Weak dependence of mobility of membrane protein aggregates on aggregate size supports a viscous model of retardation of diffusion

AU - Kucik, Dennis F.

AU - Elson, Elliot L.

AU - Sheetz, Michael

PY - 1999/1/1

Y1 - 1999/1/1

N2 - Proteins in plasma membranes diffuse more slowly than proteins inserted into artificial lipid bilayers. On a long-range scale (>250 nm), submembrane barriers, or skeleton fences that hinder long-range diffusion and create confinement zones, have been described. Even within such confinement zones, however, diffusion of proteins is much slower than predicted by the viscosity of the lipid. The cause of this slowing of diffusion on the micro scale has not been determined and is the focus of this paper. One way to approach this question is to determine the dependence of particle motion on particle size. Some current models predict that the diffusion coefficient of a membrane protein aggregate will depend strongly on its size, while others do not. We have measured the diffusion coefficients of membrane glycoprotein aggregates linked together by concanavalin A molecules bound to beads of various sizes, and also the diffusion coefficients of individual concanavalin A binding proteins. The measurements demonstrate at most a weak dependence of diffusion coefficient on aggregate size. This finding supports retardation by viscous effects, and is not consistent with models involving direct interaction of diffusing proteins with cytoskeletal elements.

AB - Proteins in plasma membranes diffuse more slowly than proteins inserted into artificial lipid bilayers. On a long-range scale (>250 nm), submembrane barriers, or skeleton fences that hinder long-range diffusion and create confinement zones, have been described. Even within such confinement zones, however, diffusion of proteins is much slower than predicted by the viscosity of the lipid. The cause of this slowing of diffusion on the micro scale has not been determined and is the focus of this paper. One way to approach this question is to determine the dependence of particle motion on particle size. Some current models predict that the diffusion coefficient of a membrane protein aggregate will depend strongly on its size, while others do not. We have measured the diffusion coefficients of membrane glycoprotein aggregates linked together by concanavalin A molecules bound to beads of various sizes, and also the diffusion coefficients of individual concanavalin A binding proteins. The measurements demonstrate at most a weak dependence of diffusion coefficient on aggregate size. This finding supports retardation by viscous effects, and is not consistent with models involving direct interaction of diffusing proteins with cytoskeletal elements.

UR - http://www.scopus.com/inward/record.url?scp=0032946242&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0032946242&partnerID=8YFLogxK

U2 - 10.1016/S0006-3495(99)77198-5

DO - 10.1016/S0006-3495(99)77198-5

M3 - Article

C2 - 9876143

AN - SCOPUS:0032946242

VL - 76

SP - 314

EP - 322

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 1 I

ER -