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 language | English (US) |
|---|---|
| Pages (from-to) | 417-431 |
| Number of pages | 15 |
| Journal | Annual Review of Biophysics and Biomolecular Structure |
| Volume | 22 |
| DOIs | |
| State | Published - Jan 1 1993 |
| Externally published | Yes |
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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 journal › Review article
}
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 -