Glycoprotein motility and dynamic domains in fluid plasma membranes

Research output: Contribution to journalReview article

70 Citations (Scopus)

Abstract

The diffusion measurements of glycoproteins have further supported a fluid mosaic model of membrane structure, but the basis of the lower apparent diffusion coefficients in biological membranes remains incompletely understood. In the specific case of glycoproteins with a single α-helix spanning the membrane, studies indicate that the major frictional drag is in the external protein layer and not the bilayer. Only in the erythrocyte membrane does the internal protein layer clearly control the lateral diffusion coefficient of a glycoprotein with a large cytoplasmic domain. In cultured cells, the barriers to lateral displacements over long distances are primarily on the cytoplasmic surface and not in the external matrix. Active movements of individual or small groups of glycoproteins both forward and rearward on cells appear to result from the interactions with moving cytoskeletal structures. Membrane turnover as well as transient attachment to the cytoskeleton can produce dynamic domains in the membrane that would depend on motile activity. Recent technological advances enable simultaneous monitoring of specific cell functions and glycoprotein motility, making it possible to corelate membrane fluidity and active glycoprotein movements with cell function.

Original languageEnglish (US)
Pages (from-to)417-431
Number of pages15
JournalAnnual Review of Biophysics and Biomolecular Structure
Volume22
DOIs
StatePublished - Jan 1 1993
Externally publishedYes

Fingerprint

Glycoproteins
Cell membranes
Cell Membrane
Fluids
Membranes
Proteins
Biological membranes
Membrane structures
Membrane Fluidity
Fluidity
Erythrocyte Membrane
Cytoskeleton
Cell Movement
Drag
Cultured Cells
Cells
Monitoring

Keywords

  • Cell motility
  • Membrane diffusion
  • Membrane traffic

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

Glycoprotein motility and dynamic domains in fluid plasma membranes. / Sheetz, Michael.

In: Annual Review of Biophysics and Biomolecular Structure, Vol. 22, 01.01.1993, p. 417-431.

Research output: Contribution to journalReview article

@article{46982740f37d456bacbb76a14d67ef20,
title = "Glycoprotein motility and dynamic domains in fluid plasma membranes",
abstract = "The diffusion measurements of glycoproteins have further supported a fluid mosaic model of membrane structure, but the basis of the lower apparent diffusion coefficients in biological membranes remains incompletely understood. In the specific case of glycoproteins with a single α-helix spanning the membrane, studies indicate that the major frictional drag is in the external protein layer and not the bilayer. Only in the erythrocyte membrane does the internal protein layer clearly control the lateral diffusion coefficient of a glycoprotein with a large cytoplasmic domain. In cultured cells, the barriers to lateral displacements over long distances are primarily on the cytoplasmic surface and not in the external matrix. Active movements of individual or small groups of glycoproteins both forward and rearward on cells appear to result from the interactions with moving cytoskeletal structures. Membrane turnover as well as transient attachment to the cytoskeleton can produce dynamic domains in the membrane that would depend on motile activity. Recent technological advances enable simultaneous monitoring of specific cell functions and glycoprotein motility, making it possible to corelate membrane fluidity and active glycoprotein movements with cell function.",
keywords = "Cell motility, Membrane diffusion, Membrane traffic",
author = "Michael Sheetz",
year = "1993",
month = "1",
day = "1",
doi = "10.1146/annurev.bb.22.060193.002221",
language = "English (US)",
volume = "22",
pages = "417--431",
journal = "Annual Review of Biophysics",
issn = "1936-122X",
publisher = "Annual Reviews Inc.",

}

TY - JOUR

T1 - Glycoprotein motility and dynamic domains in fluid plasma membranes

AU - Sheetz, Michael

PY - 1993/1/1

Y1 - 1993/1/1

N2 - The diffusion measurements of glycoproteins have further supported a fluid mosaic model of membrane structure, but the basis of the lower apparent diffusion coefficients in biological membranes remains incompletely understood. In the specific case of glycoproteins with a single α-helix spanning the membrane, studies indicate that the major frictional drag is in the external protein layer and not the bilayer. Only in the erythrocyte membrane does the internal protein layer clearly control the lateral diffusion coefficient of a glycoprotein with a large cytoplasmic domain. In cultured cells, the barriers to lateral displacements over long distances are primarily on the cytoplasmic surface and not in the external matrix. Active movements of individual or small groups of glycoproteins both forward and rearward on cells appear to result from the interactions with moving cytoskeletal structures. Membrane turnover as well as transient attachment to the cytoskeleton can produce dynamic domains in the membrane that would depend on motile activity. Recent technological advances enable simultaneous monitoring of specific cell functions and glycoprotein motility, making it possible to corelate membrane fluidity and active glycoprotein movements with cell function.

AB - The diffusion measurements of glycoproteins have further supported a fluid mosaic model of membrane structure, but the basis of the lower apparent diffusion coefficients in biological membranes remains incompletely understood. In the specific case of glycoproteins with a single α-helix spanning the membrane, studies indicate that the major frictional drag is in the external protein layer and not the bilayer. Only in the erythrocyte membrane does the internal protein layer clearly control the lateral diffusion coefficient of a glycoprotein with a large cytoplasmic domain. In cultured cells, the barriers to lateral displacements over long distances are primarily on the cytoplasmic surface and not in the external matrix. Active movements of individual or small groups of glycoproteins both forward and rearward on cells appear to result from the interactions with moving cytoskeletal structures. Membrane turnover as well as transient attachment to the cytoskeleton can produce dynamic domains in the membrane that would depend on motile activity. Recent technological advances enable simultaneous monitoring of specific cell functions and glycoprotein motility, making it possible to corelate membrane fluidity and active glycoprotein movements with cell function.

KW - Cell motility

KW - Membrane diffusion

KW - Membrane traffic

UR - http://www.scopus.com/inward/record.url?scp=0027232839&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027232839&partnerID=8YFLogxK

U2 - 10.1146/annurev.bb.22.060193.002221

DO - 10.1146/annurev.bb.22.060193.002221

M3 - Review article

C2 - 8347996

AN - SCOPUS:0027232839

VL - 22

SP - 417

EP - 431

JO - Annual Review of Biophysics

JF - Annual Review of Biophysics

SN - 1936-122X

ER -