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The role of the gap junction protein connexin43 in B lymphocyte motility and migration
Author(s) -
Machtaler Steven,
Choi Kate,
Dang-Lawson May,
Falk Letitia,
Pournia Farnaz,
Naus Christian C.,
Matsuuchi Linda
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.01.027
Subject(s) - microbiology and biotechnology , motility , cell migration , cytoskeleton , actin cytoskeleton , biology , rap1 , cell adhesion , cell junction , actin , cell , chemistry , signal transduction , biochemistry
The gap junction family of proteins is widely expressed in mammalian cells and form intercellular channels between adjacent cells, as well as hemichannels, for transport of molecules between the cell and the surrounding environment. In addition, gap junction proteins have recently been implicated as important for the regulation of cell adhesion and migration in a variety of cell types. The gap junction protein connexin43 (Cx43) regulates B lymphocyte adhesion, BCR‐ and LFA‐1‐mediated activation of the GTPase Rap1, and cytoskeletal rearrangements resulting in changes to cell shape and membrane spreading. We demonstrate here that the actin cytoskeleton is important for the distribution of Cx43 in the B cell plasma membrane and for other cell processes involving the cytoskeleton. Using shRNA knockdown of Cx43 in B lymphoma cells we show that Cx43 is also necessary for chemokine‐mediated Rap 1 activation, motility, CXCL12‐directed migration, and movement across an endothelial cell monolayer. These results demonstrate that in addition to its role in B cell spreading, Cx43 is an important regulator of B‐cell motility and migration, processes essential for normal B‐cell development and immune responses.