BCY1/YIL033C Summary Help

Standard Name BCY1 1
Systematic Name YIL033C
Alias SRA1 2
Feature Type ORF, Verified
Description Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA); PKA is a component of a signaling pathway that controls a variety of cellular processes, including metabolism, cell cycle, stress response, stationary phase, and sporulation (3, 4 and see Summary Paragraph)
Name Description Bypass of CYclic-AMP requirement 1
Chromosomal Location
ChrIX:291669 to 290419 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Genetic position: -28 cM
Gene Ontology Annotations All BCY1 GO evidence and references
  View Computational GO annotations for BCY1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Regulators 6 genes
Resources
Classical genetics
null
unspecified
Large-scale survey
null
Resources
259 total interaction(s) for 198 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 29
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 8
  • Biochemical Activity: 11
  • PCA: 10
  • Protein-peptide: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 13

Genetic Interactions
  • Dosage Growth Defect: 1
  • Dosage Lethality: 2
  • Dosage Rescue: 18
  • Negative Genetic: 120
  • Phenotypic Enhancement: 4
  • Phenotypic Suppression: 5
  • Positive Genetic: 14
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 3
  • Synthetic Rescue: 16

Resources
Expression Summary
histogram
Resources
Length (a.a.) 416
Molecular Weight (Da) 47,219
Isoelectric Point (pI) 8.14
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrIX:291669 to 290419 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
SGD ORF map
Genetic position: -28 cM
Last Update Coordinates: 2011-02-03 | Sequence: 1994-12-10
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1251 291669..290419 2011-02-03 1994-12-10
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000001295
SUMMARY PARAGRAPH for BCY1

BCY1 encodes the regulatory subunit of cAMP-dependent protein kinase (PKA), the effector kinase of the Ras-cAMP signaling pathway (reviews of the Ras-cAMP pathway can be found in 5 and 6). PKA activity regulates processes involved in cell growth and response to nutrients and stress (reviewed in 6, 7, 8, and 9). In the absence of cAMP, Bcy1p inhibits PKA activity by forming an inactive heterotetrameric complex with the PKA catalytic subunits (encoded by TPK1, TPK2, and TPK3), in which two regulatory subunits bind to two catalytic subunits. In the presence of cAMP, binding of cAMP to Bcy1p causes its dissociation from the complex as a homodimer, releasing the catalytic subunits as two active monomer (10 and references therein).

PKA is able to phosphorylate its own regulatory subunit, and the phosphorylation state of Bcy1p has been shown to affect its affinity for the PKA catalytic subunits (11). Phosphorylation of Bcy1p by other kinases, such as Yak1p and Mck1p, affects its cellular localization. External stimuli (e.g., growth on a non-fermentable carbon source or an increase in temperature) result in these kinases phosphorylating an N-terminal localization domain in Bcy1p (12, 13, 14), and the phosphorylated form of Bcy1p translocates from the nucleus to the cytoplasm via an interaction with the protein Zds1p. Bcy1p function is independent of its location, but the relocalization of Bcy1p to the cytoplasm may serve to recruit PKA to a specific subset of target proteins (14, 15). Increased temperature also leads to higher expression of the BCY1 gene (14).

Null mutations in BCY1 lead to constitutive PKA activity, which results in such phenotypes as reduced glycogen accumulation, impaired growth on a variety of carbon sources, temperature sensitivity, and sensitivity to nitrogen starvation (3, 2). PKA is conserved from yeast to man, and BCY1 homologs have been identified in fission yeast, flies, worms, mice, pigs, cows, and humans (10, 16, and reviewed in 17). In humans, four regulatory subunit genes falling into two classes, RI and RII, have been identified, and Bcy1p is structurally and functionally similar to the mammalian RII class of PKA regulators (3, 18, and reviewed in 17).

Last updated: 2007-05-23 Contact SGD

References cited on this page View Complete Literature Guide for BCY1
1) Matsumoto K, et al.  (1982) Isolation and characterization of yeast mutants deficient in adenylate cyclase and cAMP-dependent protein kinase. Proc Natl Acad Sci U S A 79(7):2355-9
2) Cannon JF and Tatchell K  (1987) Characterization of Saccharomyces cerevisiae genes encoding subunits of cyclic AMP-dependent protein kinase. Mol Cell Biol 7(8):2653-63
3) Toda T, et al.  (1987) Cloning and characterization of BCY1, a locus encoding a regulatory subunit of the cyclic AMP-dependent protein kinase in Saccharomyces cerevisiae. Mol Cell Biol 7(4):1371-7
4) Cannon JF, et al.  (1990) Yeast cAMP-dependent protein kinase regulatory subunit mutations display a variety of phenotypes. J Biol Chem 265(20):11897-904
5) Broach JR  (1991) RAS genes in Saccharomyces cerevisiae: signal transduction in search of a pathway. Trends Genet 7(1):28-33
6) Santangelo GM  (2006) Glucose signaling in Saccharomyces cerevisiae. Microbiol Mol Biol Rev 70(1):253-82
7) Estruch F  (2000) Stress-controlled transcription factors, stress-induced genes and stress tolerance in budding yeast. FEMS Microbiol Rev 24(4):469-86
8) Norbeck J and Blomberg A  (2000) The level of cAMP-dependent protein kinase A activity strongly affects osmotolerance and osmo-instigated gene expression changes in Saccharomyces cerevisiae. Yeast 16(2):121-37
9) Barbieri M, et al.  (2003) Insulin/IGF-I-signaling pathway: an evolutionarily conserved mechanism of longevity from yeast to humans. Am J Physiol Endocrinol Metab 285(5):E1064-71
10) Toda T, et al.  (1987) Three different genes in S. cerevisiae encode the catalytic subunits of the cAMP-dependent protein kinase. Cell 50(2):277-87
11) Kuret J, et al.  (1988) Mutagenesis of the regulatory subunit of yeast cAMP-dependent protein kinase. Isolation of site-directed mutants with altered binding affinity for catalytic subunit. J Biol Chem 263(19):9149-54
12) Werner-Washburne M, et al.  (1991) Bcy1, the regulatory subunit of cAMP-dependent protein kinase in yeast, is differentially modified in response to the physiological status of the cell. J Biol Chem 266(29):19704-9
13) Griffioen G, et al.  (2000) Nutritional control of nucleocytoplasmic localization of cAMP-dependent protein kinase catalytic and regulatory subunits in Saccharomyces cerevisiae. J Biol Chem 275(2):1449-56
14) Griffioen G, et al.  (2003) Feedback inhibition on cell wall integrity signaling by Zds1 involves Gsk3 phosphorylation of a cAMP-dependent protein kinase regulatory subunit. J Biol Chem 278(26):23460-71
15) Griffioen G, et al.  (2001) Nucleocytoplasmic distribution of budding yeast protein kinase A regulatory subunit Bcy1 requires Zds1 and is regulated by Yak1-dependent phosphorylation of its targeting domain. Mol Cell Biol 21(2):511-23
16) Yu G, et al.  (1994) The Schizosaccharomyces pombe pka1 gene, encoding a homolog of cAMP-dependent protein kinase. Gene 151(1-2):215-20
17) Scott JD  (1991) Cyclic nucleotide-dependent protein kinases. Pharmacol Ther 50(1):123-45
18) Johnson KE, et al.  (1987) Expression in Escherichia coli of BCY1, the regulatory subunit of cyclic AMP-dependent protein kinase from Saccharomyces cerevisiae. Purification and characterization. J Biol Chem 262(18):8636-42