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@article{1116931, author = {Valencia, Rocio G and Walko, Gernot and Janda, Lubomír and Nováček, Jiří and Mihailovska, Eva and Reipert, Siegfried and AndraandMarobela, Kerstin and Wiche, Gerhard}, article_location = {BETHESDA}, article_number = {6}, doi = {http://dx.doi.org/10.1091/mbc.E12-06-0488}, keywords = {SUBSTRATE ADHESION DYNAMICS; EPIDERMOLYSIS-BULLOSA; MUSCULAR-DYSTROPHY; TYROSINE KINASES; VIMENTIN NETWORK; CULTURED-CELLS; PROTEINS MAP-1; GLUCOSE-UPTAKE; ALPHA-TUBULIN; TAU}, language = {eng}, issn = {1059-1524}, journal = {Molecular Biology of the Cell}, title = {Intermediate filament-associated cytolinker plectin 1c destabilizes microtubules in keratinocytes}, url = {http://www.molbiolcell.org/content/early/2013/01/28/mbc.E12-06-0488.full.pdf+html}, volume = {24}, year = {2013} }
TY - JOUR ID - 1116931 AU - Valencia, Rocio G - Walko, Gernot - Janda, Lubomír - Nováček, Jiří - Mihailovska, Eva - Reipert, Siegfried - Andra-Marobela, Kerstin - Wiche, Gerhard PY - 2013 TI - Intermediate filament-associated cytolinker plectin 1c destabilizes microtubules in keratinocytes JF - Molecular Biology of the Cell VL - 24 IS - 6 SP - 768-784 EP - 768-784 PB - AMER SOC CELL BIOLOGY SN - 10591524 KW - SUBSTRATE ADHESION DYNAMICS KW - EPIDERMOLYSIS-BULLOSA KW - MUSCULAR-DYSTROPHY KW - TYROSINE KINASES KW - VIMENTIN NETWORK KW - CULTURED-CELLS KW - PROTEINS MAP-1 KW - GLUCOSE-UPTAKE KW - ALPHA-TUBULIN KW - TAU UR - http://www.molbiolcell.org/content/early/2013/01/28/mbc.E12-06-0488.full.pdf+html L2 - http://www.molbiolcell.org/content/early/2013/01/28/mbc.E12-06-0488.full.pdf+html N2 - The transition of microtubules (MTs) from an assembled to a disassembled state plays an essential role in several cellular functions. While MT dynamics are often linked to those of actin filaments, little is known about whether intermediate filaments (IFs) have an influence on MT dynamics. We show here that plectin 1c (P1c), one of the multiple isoforms of the IF-associated cytolinker protein plectin, acts as an MT destabilizer. We found that MTs in P1c-deficient (P1c(-/-)) keratinocytes are more resistant toward nocodazole-induced disassembly and display increased acetylation. In addition, live imaging of MTs in P1c(-/-), as well as in plectin-null, cells revealed decreased MT dynamics. Increased MT stability due to P1c deficiency led to changes in cell shape, increased velocity but loss of directionality of migration, smaller-sized focal adhesions, higher glucose uptake, and mitotic spindle aberrations combined with reduced growth rates of cells. On the basis of ex vivo and in vitro experimental approaches, we suggest a mechanism for MT destabilization in which isoform-specific binding of P1c to MTs antagonizes the MT-stabilizing and assembly-promoting function of MT-associated proteins through an inhibitory function exerted by plectin's SH3 domain. Our results open new perspectives on cytolinker-coordinated IF-MT interaction and its physiological significance. ER -
VALENCIA, Rocio G, Gernot WALKO, Lubomír JANDA, Jiří NOVÁČEK, Eva MIHAILOVSKA, Siegfried REIPERT, Kerstin ANDRA-MAROBELA a Gerhard WICHE. Intermediate filament-associated cytolinker plectin 1c destabilizes microtubules in keratinocytes. \textit{Molecular Biology of the Cell}. BETHESDA: AMER SOC CELL BIOLOGY, roč.~24, č.~6, s.~768-784. ISSN~1059-1524. doi:10.1091/mbc.E12-06-0488. 2013.
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