Journal Article

FZJ-2016-00257

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Clathrin assembly regulated by adaptor proteins in coarse-grained models

Giani, M. ; den Otter, W. K. (Corresponding author) ; Briels, W.FZJ*

2016
Cell Press Cambridge, Mass.

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Please use a persistent id in citations: doi:10.1016/j.bpj.2016.06.003

Abstract: The assembly of clathrin triskelia into polyhedral cages during endocytosis is regulated by adaptor proteins (APs). We explore how APs achieve this by developing coarse-grained models for clathrin and AP2, employing a Monte Carlo click interaction, to simulate their collective aggregation behavior. The phase diagrams indicate that a crucial role is played by the mechanical properties of the disordered linker segment of AP. We also present a statistical-mechanical theory for the assembly behavior of clathrin, yielding good agreement with our simulations and experimental data from the literature. Adaptor proteins are found to regulate the formation of clathrin coats under certain conditions, but can also suppress the formation of cages.

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Contributing Institute(s):

1. Weiche Materie (ICS-3)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2016

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; No Authors Fulltext ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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