ArticleMolecular and cellular biochemistry2001
HIV-1 Rev transactivator: a beta-subunit directed substrate and effector of protein kinase CK2.
Article in Molecular and cellular biochemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.
What it found
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Who cites it
12 citing papers in PubMed, 1 synthesis or guideline pooled it, 21 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.ACS chemical biology · 2022Article
- Where all the Roads Meet? A Crossover Perspective on Host Factors Regulating SARS-CoV-2 infection.Journal of molecular biology · 2022Review
- Epigenetics, N-myrystoyltransferase-1 and casein kinase-2-alpha modulates the increased replication of HIV-1 CRF02_AG, compared to subtype-B viruses.Scientific reports · 2019Article
- The Development of CK2 Inhibitors: From Traditional Pharmacology to in Silico Rational Drug Design.Pharmaceuticals (Basel, Switzerland) · 2017Review
- Article
- Predicting CK2 beta-dependent substrates using linear patterns.Biochemistry and biophysics reports · 2015Article
- Article
- Article
- The emerging CK2 interactome: insights into the regulation and functions of CK2.Molecular and cellular biochemistry · 2008Article
- Discovering regulated networks during HIV-1 latency and reactivation.Pacific Symposium on Biocomputing. Pacific Symposium on Biocomputing · 2006Article
- Structural basis of regulation and substrate specificity of protein kinase CK2 deduced from the modeling of protein-protein interactions.BMC structural biology · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phosphorylation of HIV-1 Rev by protein kinase CK2 is strictly dependent on the regulatory beta subunit of the kinase and is deeply affected by conformational changes of the substrate outside the phosphorylation site. Here we show that Rev modulates a variety of CK2 properties, including autophosphorylation, catalytic activity toward calmodulin, and susceptibility to polycationic effectors, whose common denominator is the involvement of the beta subunit. Rev's two major CK2 sites are located at its N-terminus, immediately adjacent to a helix-loop-helix motif. By comparing the behaviour of full-size Rev with that of synthetic peptides reproducing, with suitable modifications, its N-terminal 26 amino acids including the phosphoacceptor site (Ser 5, Ser 8) and amphipathic helix-1, it appears that the functional interaction of the N-terminal portion of Rev with the N-terminal domain of the beta subunit must rely on both electrostatic and hydrophobic interactions. The former mainly involve Rev's arginine-rich domain (residues 35-50) in helix-2, while the latter are mostly mediated by residues 12-24 of helix-1. These data disclose the possibility that, besides displaying protective, regulatory and targeting properties with respect to the catalytic subunit, the CK2 beta subunit also plays a role as a docking site for a subset of CK2 substrates.
Indexed as
Identifiers
11827166W1537330292What OpenQuestion holds
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.