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Published online June 9, 2008
doi:10.1083/jcb.200710151
The Journal of Cell Biology, Vol. 181, No. 6, 903-911
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Winter et al.
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 Plectin isoform 1b mediates mitochondrion–intermediate filament network linkage and controls organelle shape

Lilli Winter, Christina Abrahamsberg, and Gerhard Wiche

Department of Molecular Cell Biology, Max F. Perutz Laboratories, University of Vienna, 1030 Vienna, Austria

Correspondence to G. Wiche: gerhard.wiche{at}univie.ac.at

Plectin is a versatile intermediate filament (IF)–bound cytolinker protein with a variety of differentially spliced isoforms accounting for its multiple functions. One particular isoform, plectin 1b (P1b), remains associated with mitochondria after biochemical fractionation of fibroblasts and cells expressing exogenous P1b. Here, we determined that P1b is inserted into the outer mitochondrial membrane with the exon 1b–encoded N-terminal sequence serving as a mitochondrial targeting and anchoring signal. To study P1b-related mitochondrial functions, we generated mice that selectively lack this isoform but express all others. In primary fibroblasts and myoblasts derived from these mice, we observe a substantial elongation of mitochondrial networks, whereas other mitochondrial properties remain largely unaffected. Normal morphology of mitochondria could be restored by isoform-specific overexpression of P1b in P1b-deficient as well as plectin-null cells. We propose a model where P1b both forms a mitochondrial signaling platform and affects organelle shape and network formation by tethering mitochondria to IFs.

Abbreviations used in this paper: ATPS, ATP synthase; cyt c, cytochrome c; IF, intermediate filament; mito-PAGFP, mitochondrial matrix–targeted photoactivatable GFP; NAO, 10-N-nonyl-acridine orange; P1b, plectin 1b; RACK1, receptor for activated C kinase 1; ROI, region of interest; vim, vimentin; wt, wild type.


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