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Neddylation and CAND1 independently stimulate SCF ubiquitin ligase activity in Candida albicans

Nadine Sela1, Avigail Atir-Lande, Daniel Kornitzer

  • 1Department of Molecular Microbiology, B Rappaport Faculty of Medicine, Technion--IIT, Haifa, Israel.

Eukaryotic Cell
|November 15, 2011
PubMed

Insights

Cullin-associated, neddylation-dissociated (CAND1) protein stimulates SCF ubiquitin ligase activity, independent of neddylation. Deleting CAND1 and Rub1/NEDD8 homologs in Candida albicans reduced SCF ligase function.

Area of Science:

  • Molecular biology
  • Biochemistry
  • Cell biology

Background:

  • SCF (Skp1-cullin/Cdc53-F-box protein) ubiquitin ligases are crucial for protein degradation.
  • Cullin subunits are regulated by neddylation (Rub1/NEDD8) and CAND1 binding.

Purpose of the Study:

  • To genetically analyze the roles of Rub1/NEDD8, CAND1, and Jab1 in Candida albicans SCF ligase function.
  • To investigate the interaction between CaTIP120 (CAND1 homolog) and CaCdc53.

Main Methods:

  • Gene deletion of CaRUB1 and CaTIP120.
  • Generation of a temperature-sensitive CaCDC53 allele.
  • Phenotypic analysis of deletion mutants (morphology, growth, protein degradation).

Main Results:

  • Deletion of CaRUB1 and CaTIP120 individually reduced SCF ubiquitin ligase activity.
  • The double Carub1(-/-) Catip120(-/-) mutant exhibited more severe defects in SCF activity.
  • CAND1 stimulates SCF activity independently of neddylation.

Conclusions:

  • CAND1 plays a significant role in stimulating SCF ubiquitin ligase activity.
  • CAND1's function is independent of the neddylation pathway.
  • CAND1 is likely involved in SCF complex remodeling, not protein protection.

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