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      SUMO Regulates the Assembly and Function of a Cytoplasmic Intermediate Filament Protein in C. elegans

      , , , , ,
      Developmental Cell
      Elsevier BV

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          Abstract

          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 approximately 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.

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          Author and article information

          Journal
          Developmental Cell
          Developmental Cell
          Elsevier BV
          15345807
          November 2009
          November 2009
          : 17
          : 5
          : 724-735
          Article
          10.1016/j.devcel.2009.10.005
          2803632
          19922876
          5ba9fcc6-c40b-48dc-ae4c-73c9bf084039
          © 2009

          https://www.elsevier.com/tdm/userlicense/1.0/

          https://www.elsevier.com/open-access/userlicense/1.0/

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