Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterized by receptor dragging by laser tweezers: fence versus tether.

Sako, Yasushi; Kusumi, Akihiro

doi:10.1083/jcb.129.6.1559

Cited by 199 publications

(165 citation statements)

References 60 publications

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“…The first was to quantify the lateral diffusion of Kv2.1 inside and outside the surface cluster. If a true fence forms the cluster, as opposed to transient interactions with scaffolding proteins, the diffusion coefficients in both surface compartments should be similar; mobile and scaffolding-protein-tethered membrane proteins often have diffusion coefficients that vary by one or two orders of magnitude (Dahan et al, 2003;Meier et al, 2001;Peran et al, 2001;Sako and Kusumi, 1995;Tardin et al, 2003). The second goal was to address the question of whether other membrane proteins can cross the cluster boundary or fence.…”

Section: Introductionmentioning

confidence: 99%

A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels

Tamkun

O’Connell

Rolig

2007

Journal of Cell Science

110

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The Kv2.1 delayed-rectifier channel trafficks to 1-3 μm2 clusters on the surface of neurons and transfected HEK cells. Single quantum dot (Qdot) tracking and FRAP approaches were used to quantify the diffusion of GFP-labeled Kv2.1 channels on the cell surface and address the mechanisms underlying the formation of these unique membrane structures. Mean square displacement analysis of single Kv2.1 channel tracks inside or outside the surface clusters yielded mean diffusion coefficients of 0.03±0.02 μm2/second and 0.06±0.05 μm2/second, respectively. Kv2.1 channels outside the clusters effectively ignore the cluster boundary, readily diffusing through these microdomains. However, in 5% of the tracks analyzed, single, non-clustered channels were observed to cross into a cluster and become corralled within the cluster perimeter. Alexa Fluor 594-labelled phalloidin staining and mCherry-Kv2.1 co-expression with GFP-actin indicated that the Kv2.1 surface clusters form where the cortical actin cytoskeleton is reduced. Kv2.1 channels lacking the C-terminus do not form clusters, freely diffusing over the cell surface with a mean diffusion coefficient of 0.07±0.04 μm2/second. These data support a model whereby the Kv2.1 clusters are formed by sub-membrane cytoskeletal structures that limit the lateral diffusion of only the sub-population of Kv2.1 channels carrying the appropriate modifications on the Kv2.1 C-terminus.

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Section: Introductionmentioning

confidence: 99%

A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels

Tamkun

O’Connell

Rolig

2007

Journal of Cell Science

110

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“…The SBMS has been suggested to facilitate membrane stability and cell polarity by limiting the lateral diffusion of proteins to sites of endocytosis and as a physical barrier to clathrin pit formation (Hammerton et al, 1991;Sako and Kusumi, 1995;Kamal et al, 1998). In addition, a few reports of binding between SBMS proteins and endocytic components have also hinted at a more active role for the SBMS during endocytosis (Cianci et al, 1995;Macoska et al, 2001;Michaely et al, 1999).…”

Section: βHeavy-spectrin Segment 33 Modulates Membrane Areamentioning

confidence: 99%

The C-terminal domain ofDrosophilaβHeavy-spectrin exhibits autonomous membrane association and modulates membrane area

Williams

MacIver

Klipfell

et al. 2004

Journal of Cell Science

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Current models of cell polarity invoke asymmetric cues that reorganize the secretory apparatus to induce polarized protein delivery. An important step in this process is the stabilization of the protein composition in each polarized membrane domain. The spectrin-based membrane skeleton is thought to contribute to such stabilization by increasing the half-life of many proteins at the cell surface. Genetic evidence is consistent with a negative role for Drosophila βHeavy-spectrin in endocytosis, but the inhibitory mechanism has not been elucidated. Here, we investigated the membrane binding properties of the C-terminal nonrepetitive domain of βHeavy-spectrin through its in vivo expression in transgenic flies. We found that this region is a membrane-association domain that requires a pleckstrin homology domain for full activity, and we showed for the first time that robust membrane binding by such a C-terminal domain requires additional contributions outside the pleckstrin homology. In addition, we showed that expression of the βHeavy-spectrin C-terminal domain has a potent effect on epithelial morphogenesis. This effect is associated with its ability to induce an expansion in plasma membrane surface area. The membrane expansions adopt a very specific bi-membrane structure that sequesters both the C-terminal domain and the endocytic protein dynamin. Our data provide supporting evidence for the inhibition of endocytosis by βHeavy-spectrin, and suggest that the C-terminal domain mediates this effect through interaction with the endocytic machinery. Spectrin may be an active partner in the stabilization of polarized membrane domains.

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“…The models were inspired by studies on the dynamics of membrane bound proteins that interact with the cytoskeleton (Sako & Kusumi, 1995). For simplicity, we assume that the membrane bound protein can only diffuse in one dimension.…”

Section: Example Ifthe Corral and Trapping Modelsmentioning

confidence: 99%

A Robust Numerical Algorithm for Studying Biomolecular Transport Processes

Wang

Peskin

Elston

2003

Journal of Theoretical Biology

113

168

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We present a numerical algorithm that is well suited for the study of biomolecular transport processes. In the algorithm a continuous Markov process is discretized as a jump process and the jump rates are derived from local solutions of the continuous system. Consequently, the algorithm has two advantages over standard numerical methods: (1) it preserves detailed balance for equilibrium processes, (2) it is able to handle discontinuous potentials. The formulation of the algorithm also allows us to calculate the effective diffusion coefficient or, equivalently, the randomness parameter. We provide several simple examples of how to implement the algorithm. All the MATLAB functions files needed to reproduce the results presented in the article are available from www.amath.unc.edu/Faculty/telston/ matlab functions. r

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Barriers for lateral diffusion of transferrin receptor in the plasma membrane as characterized by receptor dragging by laser tweezers: fence versus tether.

Abstract: Abstract. Our previous results indicated that the plasma membrane of cultured normal rat kidney fibroblastic cell is compartmentalized for diffusion of receptor molecules, and that long-range diffusion is the result

Cited by 199 publications

References 60 publications

A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels

A cytoskeletal-based perimeter fence selectively corrals a sub-population of cell surface Kv2.1 channels

The C-terminal domain ofDrosophilaβHeavy-spectrin exhibits autonomous membrane association and modulates membrane area

A Robust Numerical Algorithm for Studying Biomolecular Transport Processes

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