ArticleProceedings of the National Academy of Sciences of the United States of America2002
Regulatory interaction of phosducin-like protein with the cytosolic chaperonin complex.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
What it found
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Who cites it
38 citing papers in PubMed, 76 citations in OpenAlex.
- The structural basis of eukaryotic chaperonin TRiC/CCT: Action and folding.Molecules and cells · 2024Review
- A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle.Nature communications · 2024Article
- Revisiting the chaperonin T-complex protein-1 ring complex in human health and disease: A proteostasis modulator and beyond.Clinical and translational medicine · 2024Review
- The evolutionarily conserved PhLP3 is essential for sperm development in Drosophila melanogaster.PloS one · 2024Article
- PDCL2 is essential for spermiogenesis and male fertility in mice.Cell death discovery · 2022Article
- Disruption of actin dynamics induces autophagy of the eukaryotic chaperonin TRiC/CCT.Cell death discovery · 2022Article
- TRiC controls transcription resumption after UV damage by regulating Cockayne syndrome protein A.Nature communications · 2018Article
- Characterization of a protozoan Phosducin-like protein-3 (PhLP-3) reveals conserved redox activity.PloS one · 2018Article
- Txndc9 Is Required for Meiotic Maturation of Mouse Oocytes.BioMed research international · 2017Article
- CCT2 Mutations Evoke Leber Congenital Amaurosis due to Chaperone Complex Instability.Scientific reports · 2016Article
- The Mechanism and Function of Group II Chaperonins.Journal of molecular biology · 2015Review
- Membrane protein transport in photoreceptors: the function of PDEδ: the Proctor lecture.Investigative ophthalmology & visual science · 2014Article
- Programmed cell death protein 5 interacts with the cytosolic chaperonin containing tailless complex polypeptide 1 (CCT) to regulate β-tubulin folding.The Journal of biological chemistry · 2014Article
- Splice isoforms of phosducin-like protein control the expression of heterotrimeric G proteins.The Journal of biological chemistry · 2013Article
- Identification of PDCL3 as a novel chaperone protein involved in the generation of functional VEGF receptor 2.The Journal of biological chemistry · 2013Article
- Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Ric-8B is a GTP-dependent G protein alphas guanine nucleotide exchange factor.The Journal of biological chemistry · 2011Article
- Modulation of phosducin-like protein 3 (PhLP3) levels promotes cytoskeletal remodelling in a MAPK and RhoA-dependent manner.PloS one · 2011Article
- Disruption of the chaperonin containing TCP-1 function affects protein networks essential for rod outer segment morphogenesis and survival.Molecular & cellular proteomics : MCP · 2011Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Phosducin and phosducin-like protein (PhLP) bind G protein betagamma subunits and regulate their activity. This report describes a previously uncharacterized binding partner unique to PhLP that was discovered by coimmunoprecipitation coupled with mass spectrometric identification. Chaperonin containing tailless complex polypeptide 1 (CCT), a cytosolic chaperone responsible for the folding of many cellular proteins, binds PhLP with a stoichiometry of one PhLP per CCT complex. Unlike protein-folding substrates of CCT, which interact only in their nonnative conformations, PhLP binds in its native state. Native PhLP competes directly for binding of protein substrates of CCT and thereby inhibits CCT activity. Overexpression of PhLP inhibited the ability of CCT to fold newly synthesized beta-actin by 80%. These results suggest that the interaction between PhLP and CCT may be a means to regulate CCT-dependent protein folding or alternatively, to control the availability of PhLP to modulate G protein signaling.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.