Association dynamics and lateral transport in biological membranes

Koppel, Dennis E.

doi:10.1002/jsscb.380170107

Cited by 27 publications

(12 citation statements)

References 18 publications

(12 reference statements)

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“…It is likely that the major reduction in the G lateral diffusion coefficients relative to the values expected in simple bilayers is due to the interactions of this protein either directly or indirectly (via other membrane proteins) with structures peripheral to the plasma membrane (10,14,15,17). For example, in VSV-infected cells, Reider et al (27) have demonstrated that the M protein in infected cells does lower the mobile fraction of G protein, but no effect on the mobility of the diffusing population was observed.…”

Section: Discussionmentioning

confidence: 99%

Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane [published erratum appers in J Cell Biol 1988 Jan;106(1):325]

Scullion¹,

Hou²,

Puddington³

et al. 1987

The Journal of Cell Biology

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Abstract. The lateral mobility of the vesicular stomatitis virus spike glycoprotein (G protein) and various mutant G proteins produced by site-directed mutagenesis of the G cDNA has been measured. Fluorescence recovery after photobleaching results for the wild type G protein in transfected COS-1 cells yielded a mean diffusion coefficient (D) of 8.5 (+ 1.3) × 10 -'1 cmVs and a mean mobile fraction of 75% (+ 3%). Eight mutant proteins were also examined: dTM14, lacking six amino acids from the transmembrane domain; TA2, lacking an oligosaccharide in the extracellular domain; QN2, possessing an extra N-linked oligosaccharide in the extracellular domain; CS2, possessing a serine instead of a cysteine at residue 489 in the cytoplasmic domain, preventing palmitate addition to the glycoprotein; TMR-stop, lacking the entire cytoplasmic domain except an arginine at residue 483; and three chimeric proteins, G~t, G23, and GHA, containing in place of the 29 amino acid wild type cytoplasmic domain the cytoplasmic domains from the surface IgM from the spike protein of the infectious bronchitis virus or from the hemagglutinin protein of the influenza virus, respectively. The mean D for the mutant proteins varied over a relatively small range, with the slowest mutant, G23, exhibiting a value of 11.3 (+ 1.4) x 10 -'1 cm2/s and the fastest mutant, GHA, having a D of 28.6 (+ 4.5) × 10-" cm2/s. The mean mobile fraction similarly varied over a small range, extending from 55 to 68 %. None of the mutations resulted in the more rapid diffusion characteristic of membrane proteins embedded in artificial bilayers. Therefore, it appears that the cytoplasmic and transmembrane domains themselves contribute little to restraining the lateral mobility of this integral membrane protein when expressed in transfected cells.

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Section: Discussionmentioning

confidence: 99%

Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane [published erratum appers in J Cell Biol 1988 Jan;106(1):325]

Scullion¹,

Hou²,

Puddington³

et al. 1987

The Journal of Cell Biology

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“…In a simpler view, microaggregation might slow lateral or rotational diffusion (the latter being relatively more sensitive to the size of the molecular aggregate (see Saffman & Delbruck, 1975;Koppel, Sheetz & Schindler, 1981;Koppel, 1981;Hughes et al, 1982), thereby affecting the rate of some surface biochemical reaction critical to triggering.…”

Section: Cell Surface Lmmunoglobulins and Immunological Responsementioning

confidence: 98%

Lateral motion of membrane proteins and biological function

Axelrod

1983

J. Membrain Biol.

183

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“…A final possibility is that antibodies bound to bilayers may associate into immobile submicroscopic clusters. If bound, clustered antibodies were in dynamic equilibrium with bound, monomeric antibodies, the second component could reflect the residency time of antibodies in immobile clusters (Koppel, 1981;Elson, 1985). The putative antibody clusters (mobile or immobile) might act as nucleation sites and precede crystallization of antibodies on phospholipid Langmuir-Blodgett films (Uzgiris and Kornberg, 1983;Uzgiris, 1986).…”

Section: Time (A)mentioning

confidence: 99%

Inhomogeneous translational diffusion of monoclonal antibodies on phospholipid Langmuir-Blodgett films

Wright¹,

Palmer²,

Thompson³

1988

Biophysical Journal

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The translational mobility of fluorescent-labeled monoclonal antibodies specifically bound to supported phospholipid bilayers containing hapten-conjugated phospholipids has been measured as a function of the surface concentration of bound antibodies using fluorescence recovery after photobleaching. Fluorescence recovery curves are fit well by a model that assumes the presence of two populations of antibodies with different lateral diffusion coefficients. The larger diffusion coefficient equals 3.5 x 10(-9) cm2/s, the smaller diffusion coefficient ranges from 1.5 x 10(-9) cm2/s to 2.5 x 10(-10) cm2/s, and the fractional fluorescence recovery associated with the smaller coefficient increases from approximately 0 to approximately 0.7 with increasing concentration of bound antibody. These results suggest that complexes of haptenated phospholipids and antibodies in phospholipid Langmuir-Blodgett films form clusters or domains in a concentration-dependent fashion.

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Association dynamics and lateral transport in biological membranes

Cited by 27 publications

References 18 publications

Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane [published erratum appers in J Cell Biol 1988 Jan;106(1):325]

Effects of mutations in three domains of the vesicular stomatitis viral glycoprotein on its lateral diffusion in the plasma membrane [published erratum appers in J Cell Biol 1988 Jan;106(1):325]

Lateral motion of membrane proteins and biological function

Inhomogeneous translational diffusion of monoclonal antibodies on phospholipid Langmuir-Blodgett films

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