Evidence map›Paper›PMID 28930676›Full record

ArticleCell reports2017

Localized Phosphorylation of a Kinesin-1 Adaptor by a Capsid-Associated Kinase Regulates HIV-1 Motility and Uncoating.

Viacheslav Malikov, Mojgan H Naghavi

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 47 citations in OpenAlex.

  1. Article
  2. Review
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  5. The HSV-1 pUL37 protein promotes cell invasion by regulating the kinesin-1 motor.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Review
  7. Review
  8. Review
  9. Capsid-host interactions for HIV-1 ingress.Microbiology and molecular biology reviews : MMBR · 2023
    Review
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  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Viacheslav MalikovDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Mojgan H NaghaviDepartment of Microbiology-Immunology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA. Electronic address: mojgan.naghavi@northwestern.edu.
Northwestern University · US

Funding

The Role of the Microtubule Regulators Kif4 and EB1 in HIV-1 InfectionP01GM105536 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI GUNDERSEN, GREGG G, NAGHAVI, MOJGAN HOSSEINI · 2014 to 2018
$7.5M
The role of amyloid precursor protein in HIV-1 replication and associated neurodegenerationR01NS099064 · NINDS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI NAGHAVI, MOJGAN HOSSEINI · 2017 to 2021
$2.1M
Characterization of the antiviral and nuclear regulatory functions of FEZ1 & NEK1R01GM101975 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI NAGHAVI, MOJGAN HOSSEINI · 2012 to 2016
$1.6M
NIGMS NIH HHS P01 GM105536NIGMS NIH HHS R01 GM101975NINDS NIH HHS R01 NS099064
6 · The paper itself

Abstract

Although microtubule motors mediate intracellular virus transport, the underlying interactions and control mechanisms remain poorly defined. This is particularly true for HIV-1 cores, which undergo complex, interconnected processes of cytosolic transport, reverse transcription, and uncoating of the capsid shell. Although kinesins have been implicated in regulating these events, curiously, there are no direct kinesin-core interactions. We recently showed that the capsid-associated kinesin-1 adaptor protein, fasciculation and elongation protein zeta-1 (FEZ1), regulates HIV-1 trafficking. Here, we show that FEZ1 and kinesin-1 heavy, but not light, chains regulate not only HIV-1 transport but also uncoating. This required FEZ1 phosphorylation, which controls its interaction with kinesin-1. HIV-1 did not stimulate widespread FEZ1 phosphorylation but, instead, bound microtubule (MT) affinity-regulating kinase 2 (MARK2) to stimulate FEZ1 phosphorylation on viral cores. Our findings reveal that HIV-1 binds a regulatory kinase to locally control kinesin-1 adaptor function on viral cores, thereby regulating both particle motility and uncoating.

Indexed as

MovementAdaptor Proteins, Signal TransducingCapsidCell LineGreen Fluorescent ProteinsHIV-1HIV InfectionsHumansKinesinsNerve Tissue ProteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesAdaptor Proteins, Signal TransducingFEZ1 protein, humanGreen Fluorescent ProteinsKinesinsMARK2 protein, humanNerve Tissue ProteinsProtein Serine-Threonine KinasescapsidFEZ1HIV-1kinesin-1MARK2traffickinguncoating

Identifiers

PMID28930676
PMCPMC5679262
OpenAlexW2754433330

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.