PLP1/YDR183W Summary Help

Standard Name PLP1 1
Systematic Name YDR183W
Feature Type ORF, Verified
Description Protein that interacts with CCT (chaperonin containing TCP-1) complex; has a role in actin and tubulin folding; has weak similarity to phosducins, which are G-protein regulators (1, 2, 3, 4 and see Summary Paragraph)
Name Description Phosducin-Like Protein 1
Chromosomal Location
ChrIV:829585 to 830277 | ORF Map | GBrowse
Gene Ontology Annotations All PLP1 GO evidence and references
  View Computational GO annotations for PLP1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
39 total interaction(s) for 33 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Affinity Capture-RNA: 2
  • Biochemical Activity: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Growth Defect: 1
  • Negative Genetic: 19
  • Synthetic Growth Defect: 7
  • Synthetic Lethality: 1
  • Synthetic Rescue: 5

Expression Summary
Length (a.a.) 230
Molecular Weight (Da) 26,622
Isoelectric Point (pI) 4.89
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrIV:829585 to 830277 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..693 829585..830277 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000002591

PLP1 is one of two S. cerevisiae genes encoding proteins similar to mammalian phosducins (1). Phosducins inhibit the GTPase activity of several heterotrimeric G proteins, presumably as a consequence of binding to the beta-gamma subunits of the G proteins (5, 6). In yeast, a heterotrimeric G protein comprising Gpa1p, Ste4p, and Ste18p transduces the mating pheromone signal (reviewed in reference 7). Both Plp1p and the second yeast phosducin, Plp2p, bind to the yeast G beta-gamma complex (Ste4p and Ste18p), suggesting that they may play a role in mating pheromone signal transduction (1). Overexpression of PLP1 or PLP2 reduces pheromone-responsive transcriptional activation, but has no effect on pheromone induced growth arrest (1). Although Plp1p is dispensable, Plp2p is essential for viability, and its essential role may be in a process other than mating (1). PLP1 exhibits genetic interactions with genes involved in folding of beta-tubulin and in assembly of alpha-beta tubulin (Tub1p-Tub2p) heterodimers, which are the basic components of microtubules (2). This suggests that Plp1p may have a role in folding of beta-tubulin, and that its similarity to phosducins may not be relevant to its biological function (2).

Last updated: 2000-04-13 Contact SGD

References cited on this page View Complete Literature Guide for PLP1
1) Flanary PL, et al.  (2000) Functional analysis of Plp1 and Plp2, two homologues of phosducin in yeast. J Biol Chem 275(24):18462-9
2) Lacefield S and Solomon F  (2003) A novel step in beta-tubulin folding is important for heterodimer formation in Saccharomyces cerevisiae. Genetics 165(2):531-41
3) Stirling PC, et al.  (2006) PhLP3 modulates CCT-mediated actin and tubulin folding via ternary complexes with substrates. J Biol Chem 281(11):7012-21
4) Dekker C, et al.  (2008) The interaction network of the chaperonin CCT. EMBO J 27(13):1827-39
5) Bauer PH, et al.  (1992) Phosducin is a protein kinase A-regulated G-protein regulator. Nature 358(6381):73-6
6) Lee RH, et al.  (1992) Regulation of retinal cGMP cascade by phosducin in bovine rod photoreceptor cells. Interaction of phosducin and transducin. J Biol Chem 267(35):25104-12
7) Sprague GF Jr and Thorner JW  (1992) "Pheromone response and signal transduction during the mating process of Saccharomyces cerevisiae." Pp. 657-744 in The Molecular and Cellular Biology of the Yeast Saccharomyces: Gene Expression, edited by Jones EW, Pringle JR and Broach JR. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press