help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Originally published as Biophys J. BioFAST on February 10, 2006.
doi:10.1529/biophysj.105.068742
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
biophysj.105.068742v1
90/9/3333    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jin, A. J.
Right arrow Articles by Nossal, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jin, A. J.
Right arrow Articles by Nossal, R.
Biophysical Journal 90:3333-3344 (2006)
© 2006 The Biophysical Society

Measuring the Elasticity of Clathrin-Coated Vesicles via Atomic Force Microscopy

Albert J. Jin *, Kondury Prasad {dagger}, Paul D. Smith *, Eileen M. Lafer {dagger} and Ralph Nossal {ddagger}

* Division of Bioengineering and Physical Science, Office of Research Services, Office of the Director, National Institutes of Health, Bethesda, Maryland; {dagger} Department of Biochemistry, University of Texas Health Science Center at San Antonio, San Antonio, Texas; and {ddagger} Laboratory of Integrative & Medical Biophysics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland

Correspondence: Address reprint requests to Ralph Nossal, E-mail: nossalr{at}mail.nih.gov; or Albert Jin, E-mail: jina{at}mail.nih.gov.

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.




This article has been cited by other articles:


Home page
 Biophys. JHome page
A.-K. Awizio, F. Onofri, F. Benfenati, and E. Bonaccurso
Influence of Synapsin I on Synaptic Vesicles: An Analysis by Force-Volume Mode of the Atomic Force Microscope and Dynamic Light Scattering
Biophys. J., August 1, 2007; 93(3): 1051 - 1060.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2006 by the Biophysical Society.