The poly-SUMO2/3 protease SENP6 enables assembly of the constitutive centromere-associated network by group deSUMOylation

Frauke Liebelt, Nicolette S. Jansen, Sumit Kumar, Ekaterina Gracheva, Laura A. Claessens, Matty Verlaan- de Vries, Edwin Willemstein and Alfred C. O. Vertegaal ()
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Frauke Liebelt: Leiden University Medical Center
Nicolette S. Jansen: Leiden University Medical Center
Sumit Kumar: Leiden University Medical Center
Ekaterina Gracheva: Leiden University Medical Center
Laura A. Claessens: Leiden University Medical Center
Matty Verlaan- de Vries: Leiden University Medical Center
Edwin Willemstein: Leiden University Medical Center
Alfred C. O. Vertegaal: Leiden University Medical Center

Nature Communications, 2019, vol. 10, issue 1, 1-18

Abstract: Abstract In contrast to our extensive knowledge on ubiquitin polymer signaling, we are severely limited in our understanding of poly-SUMO signaling. We set out to identify substrates conjugated to SUMO polymers, using knockdown of the poly-SUMO2/3 protease SENP6. We identify over 180 SENP6 regulated proteins that represent highly interconnected functional groups of proteins including the constitutive centromere-associated network (CCAN), the CENP-A loading factors Mis18BP1 and Mis18A and DNA damage response factors. Our results indicate a striking protein group de-modification by SENP6. SENP6 deficient cells are severely compromised for proliferation, accumulate in G2/M and frequently form micronuclei. Accumulation of CENP-T, CENP-W and CENP-A to centromeres is impaired in the absence of SENP6. Surprisingly, the increase of SUMO chains does not lead to ubiquitin-dependent proteasomal degradation of the CCAN subunits. Our results indicate that SUMO polymers can act in a proteolysis-independent manner and consequently, have a more diverse signaling function than previously expected.

Date: 2019
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DOI: 10.1038/s41467-019-11773-x

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