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Journal of Cell Science 115, e2104-e2104 (2002)
Copyright © 2002 The Company of Biologists Limited
doi:


In this issue

Reversible cytokeratin remodelling


Cytokeratin (CK) intermediate filaments form a dynamic network in which CK subunits continually exchange over the entire surface. Remodelling of this network is essential for mitosis, cell migration and changes in cell morphology, but the underlying mechanisms remain uncharacterized — as do those that generate the granular CK aggregates characteristic of various diseases. Rudolf Leube and co-workers now reveal that tyrosine phosphorylation plays an important role (see p. 4133). They show that treatment of cells expressing a CK13-GFP fusion protein with the tyrosine phosphatase inhibitor orthovanadate leads to rapid disassembly of CK filaments and formation of granular CK aggregates containing the crosslinking protein plectin. They also show that CK from these aggregates is reincorporated into filaments within minutes of orthovanadate removal. Interestingly, treatment of cells with okadaic acid, a serine/threonine phosphatase inhibitor, also generates CK granules, but the process is not reversible and the aggregates produced do not contain plectin. It is thus tyrosine phosphorylation that drives reversible restructuring of the cellular CK network, and plectin might do more than just crosslink filaments.


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Related articles in JCS:

Induction of rapid and reversible cytokeratin filament network remodeling by inhibition of tyrosine phosphatases
Pavel Strnad, Reinhard Windoffer, and Rudolf E. Leube
JCS 2002 115: 4133-4148. [Abstract] [Full Text]  




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