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1
*
Department of Clinical Medicine, University of Dublin, Trinity College, Dublin, Ireland; and
Royal College of Surgeons, Dublin, Ireland
T cells activated via integrin receptors can polarize and start
crawling locomotion with repeated cycles of cytoskeletal reassembly
processes, many of which depend on phosphorylation. We demonstrate that
protein kinase C (PKC) activation represents an essential event in
induction of active T cell motility. We find that in crawling T cells
triggered via cross-linking of integrin LFA-1 two PKC isoenzymes,
ß(I) and 
, are targeted to the cytoskeleton with specific
localization corresponding to the microtubule-organizing center (MTOC)
and microtubules, as detected by immunocytochemistry and
immunoblotting. Clustering of LFA-1 associated with its signaling
function also occurs at the membrane sites adjacent to the MTOC. We
further show that cells of a PKC-ß-deficient clone derived from
parental PKC-ß-expressing T cell line can neither crawl nor develop a
polarized microtubule array upon integrin cross-linking. However, their
adhesion and formation of actin-based pseudopodia remain unaffected.
Our data demonstrate the critical importance of the microtubule
cytoskeleton in T cell locomotion and suggest a novel
microtubule-directed intracellular signaling pathway mediated by
integrins and involving two distinctive PKC
isoforms.
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