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First published online 20 October 2009
doi: 10.1242/jcs.047266
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Short Report |

1 Cancer Research UK Cambridge Research Institute, Li Ka Shing Centre, Robinson Way, Cambridge, CB2 0RE, UK
2 Wellcome Trust Centre for Stem Cell Research, Tennis Court Road, Cambridge CB2 1QR, UK
3 National Cancer Research Institute, 61 Lincoln's Inn Fields, PO Box 123, London, WC2A 3PX, UK
Author for correspondence (fiona.watt{at}cancer.org.uk)
Accepted 2 September 2009
Summary
Kazrin is a widely expressed, evolutionarily conserved cytoplasmic protein that binds the cytolinker protein periplakin. Multiple functions of kazrin have been reported, including regulation of desmosome assembly, embryonic tissue morphogenesis and epidermal differentiation. Here, we identify kazrinE as a kazrin isoform that contains a liprin-homology domain (LHD) and forms complexes with kazrinA, kazrinB and kazrinC. As predicted from the presence of the LHD, kazrinE can associate with the leukocyte common antigen-related (LAR) protein tyrosine phosphatase in a phosphorylation-dependent manner. When overexpressed in epidermal keratinocytes, kazrinE induces changes in cell shape and stimulates terminal differentiation. Like the other kazrin isoforms, kazrinE localises to the nucleus and desmosomes. However, in addition, kazrinE associates with stabilised microtubules via its LHD. During terminal differentiation, the keratinocyte microtubule network undergoes extensive reorganisation; in differentiating keratinocytes, endogenous kazrinE colocalises with microtubules, but periplakin does not. We speculate that the kazrinE-microtubule interaction contributes to the mechanism by which kazrin regulates desmosome formation and epidermal differentiation.
Key words: Plakins, Liprins, Epidermis, LAR, Microtubules
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