PLP2/YOR281C Summary Help

Standard Name PLP2 1
Systematic Name YOR281C
Feature Type ORF, Verified
Description Protein that interacts with the CCT complex to stimulate actin folding; has similarity to phosducins; null mutant lethality is complemented by mouse phosducin-like protein MgcPhLP; CCT is short for chaperonin containing TCP-1; essential gene (1, 2, 3, 4 and see Summary Paragraph)
Name Description Phosducin-Like Protein 1
Chromosomal Location
ChrXV:847129 to 846269 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gene Ontology Annotations All PLP2 GO evidence and references
  View Computational GO annotations for PLP2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Classical genetics
Large-scale survey
reduction of function
35 total interaction(s) for 29 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 12
  • Affinity Capture-RNA: 3
  • Biochemical Activity: 2
  • Reconstituted Complex: 2
  • Two-hybrid: 4

Genetic Interactions
  • Dosage Rescue: 8
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2

Expression Summary
Length (a.a.) 286
Molecular Weight (Da) 32,793
Isoelectric Point (pI) 4.44
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXV:847129 to 846269 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..861 847129..846269 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 SGDIDS000005807

PLP2 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).

Plp2p is essential for viability, but the other phosducin-related protein, Plp1p, is not (1). In yeast, a heterotrimeric G protein comprising Gpa1p, Ste4p, and Ste18p transduces the mating pheromone signal (reviewed in reference 7). Both Plp1p and 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). Deletion of STE7, which encodes a MAP kinase kinase involved in pheromone signal transduction downstream of the heterotrimeric G protein (7) does not rescue the plp2 null mutant, suggesting that Plp2p may have an essential role in a process other than mating (1).

Last updated: 2000-04-13 Contact SGD

References cited on this page View Complete Literature Guide for PLP2
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) Lopez P, et al.  (2003) A novel germ line-specific gene of the phosducin-like protein (PhLP) family. A meiotic function conserved from yeast to mice. J Biol Chem 278(3):1751-7
3) Dekker C, et al.  (2008) The interaction network of the chaperonin CCT. EMBO J 27(13):1827-39
4) McCormack EA, et al.  (2009) Yeast phosducin-like protein 2 acts as a stimulatory co-factor for the folding of actin by the chaperonin CCT via a ternary complex. J Mol Biol 391(1):192-206
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