Lateral Diffusion of Visual Pigment in Photoreceptor Disk Membranes

Liebman, Paul A.; Entine, G.

doi:10.1126/science.185.4149.457

Cited by 288 publications

(136 citation statements)

References 13 publications

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“…Whether this discrepancy is due to membrane protein interactions with the cytoskeleton, to membrane topology, or to some other factor is not clear. It is interesting to note, however, that lateral diffusion coefficients of rhodopsin in rod outer segments (41,42) and protein surface antigens in unfertilized mouse ova (27) are at least 10-fold larger than the protein diffusion coef-ficients reported here and are more nearly consistent with the hydrodynamic predictions based on estimates of lipid viscosity.…”

Section: Discussionsupporting

confidence: 75%

Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes

Dragsten

Henkart

Blumenthal

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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Fluorescence photobleaching recovery was used to measure the lateral diffusion coefficient and mobile fraction of surface immunoglobulin (sIg), Thy-1 antigen, and a lipid probe in the plasma membrane of mouse lymphocytes. The lipid probe (3,3'-dioctadecylindocarbocyanine) had a mean (+SD) diffusion coefficient of (1.7 ± 0.3) X 10-8 cm2/sec, with essentially all of the probe mobile in the membrane. We detected little or no effect on the diffusion of this probe due to the presence of microvilli. Its diffusion was slightly restricted in capped regions. No differences in lipid probe mobility were detected between T and B cells. Fifty to 90% of the detectable sIg and Thy-1 antigen was free to move in the plane of the membrane with diffusion coefficients of t3 X 10-10 cm2/sec; the remainder was immobile. Crosslinking of slg with anti-Ig antibodies (in the presence of azide to inhibit capping) completely immobilized slg at high concentrations but failed to do so at low concentrations. Thy-1 antigen could not be immobilized with an IgG rabbit anti-mouse brain reagent without an additional layer of crosslinking antibody. In parallel labelings (in the absence of azide), capping of slg and Thy-1 antigen was observed only under crosslinking conditions sufficient to immobilize the membrane antigen. Sodium azide, colchicine, and cytochalasin B had no measurable effect on lipid probe, sIg, orIt is well established that many membrane components can move laterally in the plasma membrane (1, 2). In a number of systems, this lateral mobility has proved to be physiologically important: (i) histamine release by mast cells results from aggregation of Fc receptors for IgE on the cell surface (3-6); (ii) receptors for insulin and epidermal growth factor quickly aggregate on the cell surface after hormone binding, and many insulin-like actions are mimicked by the aggregation of insulin receptors with bivalent anti-insulin receptor antibodies in the absence of the hormone (7-9); (iii) lymphocytes can be stimulated to differentiate and proliferate by bivalent anti-Ig and also by lectins (10-15), which presumably aggregate particular membrane glycoproteins.An additional example of lateral movement of membrane components is provided by the capping process. Surface immunoglobulin (sIg), the antigen receptor on B lymphocytes, forms patches which then move toward one pole of the cell to form a cap when treated with bivalent anti-Ig. This also occurs upon exposure of polyvalent antigens to B 5163The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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Section: Discussionsupporting

confidence: 75%

Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes

Dragsten

Henkart

Blumenthal

et al. 1979

Proc. Natl. Acad. Sci. U.S.A.

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“…The lateral diffusion coefficient (D R ) reported for EGFR is about 1-2⅐10 Ϫ10 cm 2 s Ϫ1 (46), in line with the values determined for various membrane proteins, which are typically in the range of 5⅐10 Ϫ9 to 10 Ϫ10 cm 2 s Ϫ1 (47)(48)(49). Substituting the reported value of D R into equations for diffusion-limited rate constants in two dimensions (50 -53) and relating the collision rate to a unit of cytoplasmic water volume, we calculated the diffusion limit for the second-order rate constant k 2 to be 1-0.02 nM Ϫ1 s Ϫ1 .…”

Section: Derivation Of a Kinetic Modelsupporting

confidence: 51%

Quantification of Short Term Signaling by the Epidermal Growth Factor Receptor

Kholodenko¹,

Demin²,

Moehren³

et al. 1999

Journal of Biological Chemistry

537

606

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During the past decade, our knowledge of molecular mechanisms involved in growth factor signaling has proliferated almost explosively. However, the kinetics and control of information transfer through signaling networks remain poorly understood. This paper combines experimental kinetic analysis and computational modeling of the short term pattern of cellular responses to epidermal growth factor (EGF) in isolated hepatocytes. The experimental data show transient tyrosine phosphorylation of the EGF receptor (EGFR) and transient or sustained response patterns in multiple signaling proteins targeted by EGFR. Transient responses exhibit pronounced maxima, reached within 15-30 s of EGF stimulation and followed by a decline to relatively low (quasi-steady-state) levels. In contrast to earlier suggestions, we demonstrate that the experimentally observed transients can be accounted for without requiring receptor-mediated activation of specific tyrosine phosphatases, following EGF stimulation. The kinetic model predicts how the cellular response is controlled by the relative levels and activity states of signaling proteins and under what conditions activation patterns are transient or sustained. EGFR signaling patterns appear to be robust with respect to variations in many elemental rate constants within the range of experimentally measured values. On the other hand, we specify which changes in the kinetic scheme, rate constants, and total amounts of molecular factors involved are incompatible with the experimentally observed kinetics of signal transfer. Quantitation of signaling network responses to growth factors allows us to assess how cells process information controlling their growth and differentiation.

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“…Compared to N-4-nitrobenzo-2-oxa-1,3-diazole phosphatidylethanolamine, it diffuses at a rate near the predicted theoretical limit for a freely diffusing membrane protein (32)(33)(34) . Similar diffusion coefficients have been measured for rhodopsin in amphibian rod outer segment disks (35,36), and for plasma membrane proteins in membranes in which an underlying cytoskeleton may be modified or is separated from the membrane (37)(38)(39)(40)(41)(42) . It is not known whether a membrane-associated cytoskeleton is present in the posterior tail of guinea pig sperm .…”

Section: Rapid Communicationsmentioning

confidence: 50%

A localized surface protein of guinea pig sperm exhibits free diffusion in its domain.

Myles¹,

Primàkoff²,

Koppel³

1984

The Journal of Cell Biology

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Using the technique of fluorescence redistribution after photobleaching, we are studying the cellular mechanisms involved in localizing surface molecules to particular domains . A number of antigens localized to discrete surface regions have been identified with monoclonal antibodies on guinea pig sperm cells (Primakoff, P., and D . G . Myles, 1983, Dev . Biol ., 98 :417-428) . One of these monoclonal antibodies, PT-1, binds exclusively to the posterior tail region of the sperm cell surface . PT-1 recognizes an integral membrane protein that in complex with n-octyl-ß-D-glucopyranoside has a sedimentation coefficient of 6 .8S in sucrose density gradients . Fluorescence redistribution after photobleaching measurements reveal that within its surface domain the PT-1 antigen diffuses rapidly (D = 2 .5 x 10 -9 Cm 2/s) and completely (>90% recovery after bleaching) . These results rule out for this membrane protein all models that invoke immobilization as a mechanism for maintaining localization . We propose that the mechanism for localization of the PT-1 antigen may be a barrier to diffusion at the domain boundary .The restriction of cell surface molecules into specific domains has been well established for a wide variety of mammalian cell types . These include acetylcholine receptors at the synapse on muscle cells (1), low density lipoprotein and asialoglycoprotein receptors in coated pits of fibroblasts (2) and hepatocytes (3) and more extensive localized domains on the surface of sperm (4, 5), intestinal epithelial cells-(6, 7), and hepatocytes (8, 9). Although topographical localization of various surface receptors has been widely described, little is known concerning the mechanisms that maintain surface protein localizations . Immobilization in the membrane is a potential mechanism for maintaining a non-uniform distribution of surface molecules, and in the case of the acetylcholine receptor, it has been shown that clustered receptors are immobilized (10).In the current study we have addressed the question whether there are mechanisms other than immobilization to localize surface molecules . We have used the guinea pig sperm cell . Previously, the existence of five different antigen domains on the surface of the guinea pig sperm was established with monoclonal antibodies directed to surface antigens. These antigens may be restricted to the anterior head, posterior head, whole head, whole tail, or posterior tail cell surface (11). In some cases, patching of localized sperm surface molecules can be induced, suggesting that these molecules may be mobile in the plane of the membrane (12-15) . However, ability to patch may not be a reliable indicator of mobility of a receptor in the membrane (16-18) and gives no measure of the diffusion rate or percent mobile fraction. Therefore, we RAPID COMMUNICATIONS have directly measured these parameters using fluorescence redistribution after photobleaching of a localized sperm surface antigen that can be patched . This antigen, identified by the monoclonal antibody PT-...

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Lateral Diffusion of Visual Pigment in Photoreceptor Disk Membranes

Cited by 288 publications

References 13 publications

Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes

Lateral diffusion of surface immunoglobulin, Thy-1 antigen, and a lipid probe in lymphocyte plasma membranes

Quantification of Short Term Signaling by the Epidermal Growth Factor Receptor

A localized surface protein of guinea pig sperm exhibits free diffusion in its domain.

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