TY  - JOUR
A1  - Harwardt, Marie-Lena I. E.
A1  - Young, Phoebe
A1  - Bleymüller, Willem M.
A1  - Meyer, Timo
A1  - Karathanasis, Christos
A1  - Niemann, Hartmut H.
A1  - Heilemann, Mike
A1  - Dietz, Marina
T1  - Membrane dynamics of resting and internalin B‐bound MET receptor tyrosine kinase studied by single‐molecule tracking
T2  - FEBS Open Bio
N2  - The human MET receptor tyrosine kinase contributes to vertebrate development and cell proliferation. As a proto‐oncogene, it is a target in cancer therapies. MET is also relevant for bacterial infection by Listeria monocytogenes and is activated by the bacterial protein internalin B. The processes of ligand binding, receptor activation, and the diffusion behavior of MET within the plasma membrane as well as its interconnections with various cell components are not fully understood. We investigated the receptor diffusion dynamics using single‐particle tracking and imaging fluorescence correlation spectroscopy and elucidated mobility states of resting and internalin B‐bound MET. We show that internalin B‐bound MET exhibits lower diffusion coefficients and diffuses in a more confined area in the membrane. We report that the fraction of immobile receptors is larger for internalin B‐bound receptors than for resting MET. Results of single‐particle tracking in cells treated with various cytotoxins depleting cholesterol from the membrane and disrupting the actin cytoskeleton and microtubules suggest that cholesterol and actin influence MET diffusion dynamics, while microtubules do not have any effect.
KW  - MET receptor
KW  - diffusion dynamics
KW  - endocytosis
KW  - internalin B
KW  - receptor tyrosine kinases
KW  - single‐molecule tracking
Y1  - 2017
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/46372
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-463724
SN  - 2211-5463
N1  - © 2017 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
VL  - 7
IS  - 9
SP  - 1422
EP  - 1440
PB  - Elsevier on behalf of the Federation of European Biochemical Societies
CY  - Cambridge
ER  -