 |
PDBsum entry 4i1q
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Cell adhesion
|
PDB id
|
|
|
|
4i1q
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Bin2 is a membrane sculpting n-Bar protein that influences leucocyte podosomes, Motility and phagocytosis.
|
|
|
Authors
|
|
M.J.Sánchez-Barrena,
Y.Vallis,
M.R.Clatworthy,
G.J.Doherty,
D.B.Veprintsev,
P.R.Evans,
H.T.Mcmahon.
|
|
|
Ref.
|
|
Plos One, 2012,
7,
e52401.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Cell motility, adhesion and phagocytosis are controlled by actin and membrane
remodelling processes. Bridging integrator-2 (Bin2) also called Breast
cancer-associated protein 1 (BRAP1) is a predicted N-BAR domain containing
protein with unknown function that is highly expressed in leucocytic cells. In
the present study we solved the structure of Bin2 BAR domain and studied its
membrane binding and bending properties in vitro and in vivo. Live-cell imaging
experiments showed that Bin2 is associated with actin rich structures on the
plasma membrane, where it was targeted through its N-BAR domain. Pull-down
experiments and immunoprecipitations showed that Bin2 C-terminus bound SH3
domain containing proteins such as Endophilin A2 and α-PIX. siRNA of endogenous
protein led to decreased cell migration, increased phagocytosis and reduced
podosome density and dynamics. In contrast, overexpression of Bin2 led to
decreased phagocytosis and increased podosome density and dynamics. We conclude
that Bin2 is a membrane-sculpting protein that influences podosome formation,
motility and phagocytosis in leucocytes. Further understanding of this protein
may be key to understand the behaviour of leucocytes under physiological and
pathological conditions.
|
|
|
|
|
|
|
