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Traffic. 2015 May;16(5):519-33. doi: 10.1111/tra.12263. Epub 2015 Feb 24.

Effect of clathrin light chains on the stiffness of clathrin lattices and membrane budding.

Author information

1
Institute of Cell Biology, Centre of Anatomy, Hannover Medical School, Carl-Neuberg Street 1, D-30625, Hannover, Germany.

Abstract

Clathrin-dependent transport processes require the polymerization of clathrin triskelia into polygonal scaffolds. Together with adapter proteins, clathrin collects cargo and induces membrane bud formation. It is not known to what extent clathrin light chains affect the structural and functional properties of clathrin lattices and the ability of clathrin to deform membranes. To address these issues, we have developed a novel procedure for analyzing clathrin lattice formation on rigid surfaces. We found that lattices can form on adaptor-coated convex-, planar- and even shallow concave surfaces, but the rate of formation and resistance to thermal dissociation of the lattice are greatly enhanced on convex surfaces. Atomic force microscopy on planar clathrin lattices demonstrates that the stiffness of the clathrin lattice is strictly dependent on light chains. The reduced stiffness of the lattice also compromised the ability of clathrin to generate coated buds on the surface of rigid liposomal membranes.

KEYWORDS:

Hsc70; atomic force microscopy; curvature; electron microscopy; epsin; planar lattices; uncoating

PMID:
25652138
DOI:
10.1111/tra.12263
[Indexed for MEDLINE]
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