Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera{image}

doi:10.1083/jcb.146.6.1239

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© The Rockefeller University Press, 0021-9525/1999//1239 $5.00
The Journal of Cell Biology, Volume 146, Number 6, , 1999 1239-1254

Original Article

Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera ${image}$

Rafael García-Mata^a, Zsuzsa Bebök^b, Eric J. Sorscher^b, and Elizabeth S. Sztul^a

^a Department of Cell Biology, University of Alabama at Birmingham, Birmingham, Alabama 35294
^b The Gregory Fleming James Cystic Fibrosis Research Center, University of Alabama at Birmingham, Birmingham, Alabama 35294
Department of Cell Biology, MCLM, Room 668, 1918 University Boulevard, Birmingham, AL 35294.(205) 975-9131(205) 934-1465

esztul{at}uab.edu

Formation of a novel structure, the aggresome, has been proposedto represent a general cellular response to the presence ofmisfolded proteins (Johnston, J.A., C.L. Ward, and R.R. Kopito.1998. J. Cell Biol. 143:1883–1898; Wigley, W.C., R.P.Fabunmi, M.G. Lee, C.R. Marino, S. Muallem, G.N. DeMartino,and P.J. Thomas. 1999. J. Cell Biol. 145:481–490). Totest the generality of this finding and characterize aspectsof aggresome composition and its formation, we investigatedthe effects of overexpressing a cytosolic protein chimera (GFP-250)in cells. Overexpression of GFP-250 caused formation of aggresomesand was paralleled by the redistribution of the intermediatefilament protein vimentin as well as by the recruitment of theproteasome, and the Hsp70 and the chaperonin systems of chaperones.Interestingly, GFP-250 within the aggresome appeared not tobe ubiquitinated. In vivo time-lapse analysis of aggresome dynamicsshowed that small aggregates form within the periphery of thecell and travel on microtubules to the MTOC region where theyremain as distinct but closely apposed particulate structures.Overexpression of p50/dynamitin, which causes the dissociationof the dynactin complex, significantly inhibited the formationof aggresomes, suggesting that the minus-end–directedmotor activities of cytoplasmic dynein are required for aggresomeformation. Perinuclear aggresomes interfered with correct Golgilocalization and disrupted the normal astral distribution ofmicrotubules. However, ER-to-Golgi protein transport occurrednormally in aggresome containing cells. Our results suggestthat aggresomes can be formed by soluble, nonubiquitinated proteinsas well as by integral transmembrane ubiquitinated ones, supportingthe hypothesis that aggresome formation might be a general cellularresponse to the presence of misfolded proteins.

Key Words: aggresome • p50/dynamitin • chaperones • proteasome • microtubules

1.used in this paper: CFTR, cystic fibrosis conductance transmembraneregulator; MT, microtubule; MTOC, microtubule organizing center;PS1, presenilin 1; ROI, region of interest; VSV, vesicular stomatitisvirus

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