TY - JOUR
T1 - SUMO Regulates the Assembly and Function of a Cytoplasmic Intermediate Filament Protein in C. elegans
AU - Kaminsky, Rachel
AU - Denison, Carilee
AU - Bening-Abu-Shach, Ulrike
AU - Chisholm, Andrew D.
AU - Gygi, Steven P.
AU - Broday, Limor
N1 - Funding Information:
We thank Rudolf Leube for the anti-IFB-1 antibody, Koret Hirschberg and David Broday for consulting on FRAP analysis, and Ronen Zaidel-Bar for comments on the manuscript. Some nematode strains used in this work were provided by the Caenorhabditis Genetics Center, which is funded by the NIH National Center for Research Resources (NCRR). The MH4 and MH46 monoclonal antibodies developed by the Waterston laboratory were obtained from the Developmental Studies Hybridoma Bank developed under the auspices of the NICHD and maintained by the Department of Biology, The University of Iowa, Iowa City, IA. A.D.C. acknowledges funding from the NIH (GM54657). This research was supported by grants from the Israel Science Foundation (ISF 980/06) and the Israel Cancer Research Fund (06-203-RCDA) to L.B. and National Institutes of Health (NIH) grant GM67945 to S.P.G.
PY - 2009/11/17
Y1 - 2009/11/17
N2 - Sumoylation is a reversible posttranslational modification that plays roles in many processes, including transcriptional regulation, cell division, chromosome integrity, and DNA damage response. Using a proteomics approach, we identified ∼250 candidate targets of sumoylation in C. elegans. One such target is the cytoplasmic intermediate filament (cIF) protein named IFB-1, which is expressed in hemidesmosome-like structures in the worm epidermis and is essential for embryonic elongation and maintenance of muscle attachment to the cuticle. In the absence of SUMO, IFB-1 formed ectopic filaments and protein aggregates in the lateral epidermis. Moreover, depletion of SUMO or mutation of the SUMO acceptor site on IFB-1 resulted in a reduction of its cytoplasmic soluble pool, leading to a decrease in its exchange rate within epidermal attachment structures. These observations indicate that SUMO regulates cIF assembly by maintaining a cytoplasmic pool of nonpolymerized IFB-1, and that this is necessary for normal IFB-1 function.
AB - Sumoylation is a reversible posttranslational modification that plays roles in many processes, including transcriptional regulation, cell division, chromosome integrity, and DNA damage response. Using a proteomics approach, we identified ∼250 candidate targets of sumoylation in C. elegans. One such target is the cytoplasmic intermediate filament (cIF) protein named IFB-1, which is expressed in hemidesmosome-like structures in the worm epidermis and is essential for embryonic elongation and maintenance of muscle attachment to the cuticle. In the absence of SUMO, IFB-1 formed ectopic filaments and protein aggregates in the lateral epidermis. Moreover, depletion of SUMO or mutation of the SUMO acceptor site on IFB-1 resulted in a reduction of its cytoplasmic soluble pool, leading to a decrease in its exchange rate within epidermal attachment structures. These observations indicate that SUMO regulates cIF assembly by maintaining a cytoplasmic pool of nonpolymerized IFB-1, and that this is necessary for normal IFB-1 function.
KW - CELLBIO
KW - DEVBIO
UR - https://www.scopus.com/pages/publications/71549169907
U2 - 10.1016/j.devcel.2009.10.005
DO - 10.1016/j.devcel.2009.10.005
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C2 - 19922876
AN - SCOPUS:71549169907
SN - 1534-5807
VL - 17
SP - 724
EP - 735
JO - Developmental Cell
JF - Developmental Cell
IS - 5
ER -