Evidence map›Paper›PMID 29872222›Full record

ArticleOncogene2018

Functional characterization of lysosomal interaction of Akt with VRK2.

Noriyuki Hirata, Futoshi Suizu, Mami Matsuda-Lennikov, Tsutomu Tanaka, Tatsuma Edamura, Satoko Ishigaki, Thoria Donia, Pathrapol Lithanatudom, Chikashi Obuse, Toshihiko Iwanaga and 1 more

Open access · hybridAbstract read
In one paragraph

Article in Oncogene, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
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  4. Phafins Are More Than Phosphoinositide-Binding Proteins.International journal of molecular sciences · 2023
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  7. BackboneBiomolecular NMR assignments · 2022
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  12. Mitophagy in Diabetic Cardiomyopathy: Roles and Mechanisms.Frontiers in cell and developmental biology · 2021
    Review
  13. Article
  14. Review
  15. Article
  16. The FBXW2-MSX2-SOX2 axis regulates stem cell property and drug resistance of cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. Review
  19. Molecular neuropsychiatry · 2018
    Review
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

11 authors at 3 institutions in 2 countries.

Noriyuki HirataDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Futoshi SuizuDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Mami Matsuda-LennikovDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Tsutomu TanakaDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Tatsuma EdamuraDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Satoko IshigakiDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Thoria DoniaDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Pathrapol LithanatudomDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Chikashi ObuseDivision of Molecular Life Science, Graduate School of Life Science, Hokkaido University, Sapporo, Japan.
Toshihiko IwanagaLaboratory of Histology and Cytology, Hokkaido University Graduate School of Medicine, Sapporo, Japan.
Masayuki NoguchiDivision of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan. m_noguch@igm.hokudai.ac.jp.
Hokkaido University · JPHokkai Gakuen University · JPTanta University · EG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Serine-threonine kinase Akt (also known as PKB, protein kinase B), a core intracellular mediator of cell survival, is involved in various human cancers and has been suggested to play an important role in the regulation of autophagy in mammalian cells. Nonetheless, the physiological function of Akt in the lysosomes is currently unknown. We have reported previously that PtdIns(3)P-dependent lysosomal accumulation of the Akt-Phafin2 complex is a critical step for autophagy induction. Here, to characterize the molecular function of activated Akt in the lysosomes in the process of autophagy, we searched for the molecules that interact with the Akt complex at the lysosomes after induction of autophagy. By time-of-flight-mass spectrometry (TOF/MS) analysis, kinases of the VRK family, a unique serine-threonine family of kinases in the human kinome, were identified. VRK2 interacts with Akt1 and Akt2, but not with Akt3; the C terminus of Akt and the N terminus of VRK2 facilitate the interaction of Akt and VRK2 in mammalian cells. The kinase-dead form of VRK2A (KD VRK2A) failed to interact with Akt in coimmunoprecipitation assays. Bimolecular fluorescence complementation (BiFC) experiments showed that, in the lysosomes, Akt interacted with VRK2A but not with VRK2B or KD VRK2A. Immunofluorescent assays revealed that VRK2 and phosphorylated Akt accumulated in the lysosomes after autophagy induction. WT VRK2A, but not KD VRK2A or VRK2B, facilitated accumulation of phosphorylated Akt in the lysosomes. Downregulation of VRK2 abrogated the lysosomal accumulation of phosphorylated Akt and impaired nuclear localization of TFEB; these events coincided to inhibition of autophagy induction. The VRK2-Akt complex is required for control of lysosomal size, acidification, bacterial degradation, and for viral replication. Moreover, lysosomal VRK2-Akt controls cellular proliferation and mitochondrial outer-membrane stabilization. Given the roles of autophagy in the pathogenesis of human cancer, the current study provides a novel insight into the oncogenic activity of VRK2-Akt complexes in the lysosomes via modulation of autophagy.

Indexed as

AutophagyCell LineCell ProliferationHumansLysosomesProtein BindingProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktVRK2 protein, human

Identifiers

PMID29872222
PMCPMC6172193
OpenAlexW2805153560

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.