Journal
MOLECULAR MICROBIOLOGY
Volume 84, Issue 3, Pages 530-549Publisher
WILEY
DOI: 10.1111/j.1365-2958.2012.08042.x
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Funding
- European Union [EUROFUNG N QLK3-CT1999-00729]
- Direction des Relations Internacionales (Universite Paris-Sud)
- Agencia Espanola de Cooperacion Internacional (Spain)
- NCSR Demokritos (Greece)
- EUROFUNG contract
- Universite Paris-Sud
- CNRS
- Institut Universitaire de France
- DGCYT [BIO2009-BIO20097281]
- Comunidad de Madrid [S2006/SAL-0246]
- Royal Society
- Science Research Council
- Wellcome Trust [084660/Z/08/Z]
- Wellcome Trust [084660/Z/08/Z] Funding Source: Wellcome Trust
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Type I casein kinases are highly conserved among Eukaryotes. Of the two Aspergillus nidulans casein kinases I, CkiA is related to the d/e mammalian kinases and to Saccharomyces cerevisi ae Hrr25p. CkiA is essential. Three recessive ckiA mutations leading to single residue substitutions, and downregulation using a repressible promoter, result in partial loss-of-function, which leads to a pleiotropic defect in amino acid utilization and resistance to toxic amino acid analogues. These phenotypes correlate with miss-routing of the YAT plasma membrane transporters AgtA (glutamate) and PrnB (proline) to the vacuole under conditions that, in the wild type, result in their delivery to the plasma membrane. Miss-routing to the vacuole and subsequent transporter degradation results in a major deficiency in the uptake of the corresponding amino acids that underlies the inability of the mutant strains to catabolize them. Our findings may have important implications for understanding how CkiA, Hrr25p and other fungal orthologues regulate the directionality of transport at the ER-Golgi interface.
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