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First published online 2 August 2005
doi: 10.1242/jcs.02510


Journal of Cell Science 118, 3727-3738 (2005)
Published by The Company of Biologists 2005
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Research Article

Microtubule actin crosslinking factor 1b: a novel plakin that localizes to the Golgi complex

Chung-Ming Lin1, Hui-Jye Chen1, Conrad L. Leung1, David A. D. Parry2 and Ronald K. H. Liem1,*

1 Department of Pathology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA
2 Institute of Fundamental Sciences, Massey University, Private Bag 11 222, Palmerston North, New Zealand

* Author for correspondence (e-mail: rkl2{at}columbia.edu)

Accepted 23 May 2005

MACF1 (microtubule actin crosslinking factor), also called ACF7 (actin crosslinking family 7) is a cytoskeletal linker protein that can associate with both actin filaments and microtubules. We have identified a novel alternatively spliced isoform of MACF1. We named this isoform MACF1b and renamed the original isoform MACF1a. MACF1b is identical to MACF1a, except that it has a region containing plakin (or plectin) repeats in the middle of the molecule. MACF1b is ubiquitously expressed in adult tissues with especially high levels in the lung. We studied the subcellular localization of MACF1b proteins in mammalian cell lines. In two lung cell lines, MACF1b was chiefly localized to the Golgi complex. Upon treatments that disrupt the Golgi complex, MACF1b redistributed into the cytosol, but remained co-localized with the dispersed Golgi ministacks. MACF1b proteins can be detected in the enriched Golgi fraction by western blotting. The domain of MACF1b that targets it to the Golgi was found at the N-terminal part of the region that contains the plakin repeats. Reducing the level of MACF1 proteins by small-interfering RNA resulted in the dispersal of the Golgi complex.

Key words: plakin, cytoskeleton, microtubules, Golgi complex




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