Tankyrase-1 assembly to large protein complexes blocks its telomeric function

Kaori Hatsugai, Tomokazu Ohishi, Yoshikazu Sugimoto, Hiroyuki Seimiya

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Tankyrase-1 poly(ADP-ribosyl)ates the telomere-binding protein TRF1. This post-translational modification dissociates TRF1 from telomeres, enhancing telomerase-mediated telomere elongation. Tankyrase-1 multimerizes via its sterile alpha motif domain, but its functional implication remains elusive. Here, we found that excessive amounts of tankyrase-1 form punctate nuclear foci. This focus formation depends on both homophilic multimerization and heterophilic protein-protein interaction. These foci are functionally dormant because they do not efficiently release TRF1 from telomeres. Consistently, hyper-overexpression of tankyrase-1 attenuates its ability to elongate telomeres. These observations suggest that tankyrase-1 assembly to large protein complexes masks its telomeric function. Structured summary: MINT- 7987689, MINT- 7987677: Tankyrase-1 (uniprotkb:. O95271) and TRF1 (uniprotkb:. P54274) colocalize (MI:. 0403) by fluorescence microscopy (MI:. 0416). MINT- 7987977: Tankyrase-1 (uniprotkb:. O95271) physically interacts (MI:. 0915) with TRF1 (uniprotkb:. P54274) by anti tag coimmunoprecipitation (MI:. 0007). MINT- 7987998: Tankyrase-1 (uniprotkb:. O95271) physically interacts (MI:. 0915) with Tankyrase-1 (uniprotkb:. O95271) by anti tag coimmunoprecipitation (MI:. 0007).

Original languageEnglish
Pages (from-to)3885-3890
Number of pages6
JournalFEBS Letters
Volume584
Issue number18
DOIs
Publication statusPublished - 2010

Fingerprint

Tankyrases
Telomere
Proteins
Telomere-Binding Proteins
Protein Multimerization
Telomerase
Fluorescence microscopy
Post Translational Protein Processing
Masks
Fluorescence Microscopy
Adenosine Diphosphate
Elongation

Keywords

  • Poly(ADP-ribose) polymerase
  • Tankyrase-1
  • Telomere
  • TRF1

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology
  • Medicine(all)

Cite this

Tankyrase-1 assembly to large protein complexes blocks its telomeric function. / Hatsugai, Kaori; Ohishi, Tomokazu; Sugimoto, Yoshikazu; Seimiya, Hiroyuki.

In: FEBS Letters, Vol. 584, No. 18, 2010, p. 3885-3890.

Research output: Contribution to journalArticle

Hatsugai, Kaori ; Ohishi, Tomokazu ; Sugimoto, Yoshikazu ; Seimiya, Hiroyuki. / Tankyrase-1 assembly to large protein complexes blocks its telomeric function. In: FEBS Letters. 2010 ; Vol. 584, No. 18. pp. 3885-3890.
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abstract = "Tankyrase-1 poly(ADP-ribosyl)ates the telomere-binding protein TRF1. This post-translational modification dissociates TRF1 from telomeres, enhancing telomerase-mediated telomere elongation. Tankyrase-1 multimerizes via its sterile alpha motif domain, but its functional implication remains elusive. Here, we found that excessive amounts of tankyrase-1 form punctate nuclear foci. This focus formation depends on both homophilic multimerization and heterophilic protein-protein interaction. These foci are functionally dormant because they do not efficiently release TRF1 from telomeres. Consistently, hyper-overexpression of tankyrase-1 attenuates its ability to elongate telomeres. These observations suggest that tankyrase-1 assembly to large protein complexes masks its telomeric function. Structured summary: MINT- 7987689, MINT- 7987677: Tankyrase-1 (uniprotkb:. O95271) and TRF1 (uniprotkb:. P54274) colocalize (MI:. 0403) by fluorescence microscopy (MI:. 0416). MINT- 7987977: Tankyrase-1 (uniprotkb:. O95271) physically interacts (MI:. 0915) with TRF1 (uniprotkb:. P54274) by anti tag coimmunoprecipitation (MI:. 0007). MINT- 7987998: Tankyrase-1 (uniprotkb:. O95271) physically interacts (MI:. 0915) with Tankyrase-1 (uniprotkb:. O95271) by anti tag coimmunoprecipitation (MI:. 0007).",
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