Association of Endophilin B1 with Cytoplasmic Vesicles.

Abstract:

:Endophilins are SH3- and BAR domain-containing proteins implicated in membrane remodeling and vesicle formation. Endophilins A1 and A2 promote the budding of endocytic vesicles from the plasma membrane, whereas endophilin B1 has been implicated in vesicle budding from intracellular organelles, including the trans-Golgi network and late endosomes. We previously reported that endophilins A1 and A2 exist almost exclusively as soluble dimers in the cytosol. Here, we present results of fluorescence fluctuation spectroscopy analyses indicating that, in contrast, the majority of endophilin B1 is present in multiple copies on small, highly mobile cytoplasmic vesicles. Formation of these vesicles was enhanced by overexpression of wild-type dynamin 2, but suppressed by expression of a catalytically inactive dynamin 2 mutant. Using dual-color heterospecies partition analysis, we identified the epidermal growth factor receptor on endophilin B1 vesicles. Moreover, a proportion of endophilin B1 vesicles also contained caveolin, whereas clathrin was almost undetectable on those vesicles. These results raise the possibility that endophilin B1 participates in dynamin 2-dependent formation of a population of transport vesicles distinct from those generated by A-type endophilins.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Li J,Barylko B,Eichorst JP,Mueller JD,Albanesi JP,Chen Y

doi

10.1016/j.bpj.2016.06.017

subject

Has Abstract

pub_date

2016-08-09 00:00:00

pages

565-576

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(16)30463-5

journal_volume

111

pub_type

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