Measuring the elasticity of clathrin-coated vesicles via atomic force microscopy

Albert J. Jin; Kondury Prasad; Paul D. Smith; Eileen M. Lafer; Ralph Nossal

doi:10.1529/biophysj.105.068742

Measuring the elasticity of clathrin-coated vesicles via atomic force microscopy

Albert J. Jin, Kondury Prasad, Paul D. Smith, Eileen M. Lafer, Ralph Nossal

Department of Biochemistry & Structural Biology

Research output: Contribution to journal › Article › peer-review

54 Scopus citations

Abstract

Using a new scheme based on atomic force microscopy (AFM), we investigate mechanical properties of clathrin-coated vesicles (CCVs). CCVs are multicomponent protein and lipid complexes of ∼100 nm diameter that are implicated in many essential cell-trafficking processes. Our AFM imaging resolves clathrin lattice polygons and provides height deformation in quantitative response to AFM-substrate compression force. We model CCVs as multilayered elastic spherical shells and, from AFM measurements, estimate their bending rigidity to be 285 ± 30 k_BT, i.e., ∼20 times that of either the outer clathrin cage or inner vesicle membrane. Further analysis reveals a flexible coupling between the clathrin coat and the membrane, a structural property whose modulation may affect vesicle biogenesis and cellular function.

Original language	English (US)
Pages (from-to)	3333-3344
Number of pages	12
Journal	Biophysical Journal
Volume	90
Issue number	9
DOIs	https://doi.org/10.1529/biophysj.105.068742
State	Published - May 2006

ASJC Scopus subject areas

Biophysics

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title = "Measuring the elasticity of clathrin-coated vesicles via atomic force microscopy",

abstract = "Using a new scheme based on atomic force microscopy (AFM), we investigate mechanical properties of clathrin-coated vesicles (CCVs). CCVs are multicomponent protein and lipid complexes of ∼100 nm diameter that are implicated in many essential cell-trafficking processes. Our AFM imaging resolves clathrin lattice polygons and provides height deformation in quantitative response to AFM-substrate compression force. We model CCVs as multilayered elastic spherical shells and, from AFM measurements, estimate their bending rigidity to be 285 ± 30 kBT, i.e., ∼20 times that of either the outer clathrin cage or inner vesicle membrane. Further analysis reveals a flexible coupling between the clathrin coat and the membrane, a structural property whose modulation may affect vesicle biogenesis and cellular function.",

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note = "Funding Information: This work was supported in part by extramural grant NS29051 (to E. M. L.) and intramural funds from the National Institutes of Health, Department of Health and Human Services. ",

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AU - Prasad, Kondury

AU - Smith, Paul D.

AU - Lafer, Eileen M.

AU - Nossal, Ralph

N1 - Funding Information: This work was supported in part by extramural grant NS29051 (to E. M. L.) and intramural funds from the National Institutes of Health, Department of Health and Human Services.

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AB - Using a new scheme based on atomic force microscopy (AFM), we investigate mechanical properties of clathrin-coated vesicles (CCVs). CCVs are multicomponent protein and lipid complexes of ∼100 nm diameter that are implicated in many essential cell-trafficking processes. Our AFM imaging resolves clathrin lattice polygons and provides height deformation in quantitative response to AFM-substrate compression force. We model CCVs as multilayered elastic spherical shells and, from AFM measurements, estimate their bending rigidity to be 285 ± 30 kBT, i.e., ∼20 times that of either the outer clathrin cage or inner vesicle membrane. Further analysis reveals a flexible coupling between the clathrin coat and the membrane, a structural property whose modulation may affect vesicle biogenesis and cellular function.

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Measuring the elasticity of clathrin-coated vesicles via atomic force microscopy

Abstract

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