Evidence map›Paper›PMID 31187393›Full record

ReviewBiological trace element research2019

Molecular Mechanisms by Which Selenoprotein K Regulates Immunity and Cancer.

Michael P Marciel, Peter R Hoffmann

Open access · greenAbstract readReview
In one paragraph

Review in Biological trace element research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 1 pooled it
5.4field-weighted citation impact, top 4% 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, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Mitochondria-ER crosstalk via MAMS: Bridging cellular homeostasis and cancer progression.Apoptosis : an international journal on programmed cell death · 2026
    Review
  5. Review
  6. Article
  7. Article
  8. Selenoprotein K at the intersection of cellular pathways.Archives of biochemistry and biophysics · 2025
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. "Alphabet" Selenoproteins: Implications in Pathology.International journal of molecular sciences · 2023
    Review
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article
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.

Michael P MarcielDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, USA.
Peter R HoffmannDepartment of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii, Honolulu, HI, USA. peterrh@hawaii.edu.
University of Hawaiʻi at Mānoa · US

Funding

UH Hilo COP A&RP20GM103466 · NIGMS · UNIVERSITY OF HAWAII AT MANOA · PI HELEN C TURNER · 2012 to 2026
$60.3M
Selenoprotein K modulates calcium-dependent signaling in immune cellsR01AI089999 · NIAID · UNIVERSITY OF HAWAII AT MANOA · PI HOFFMANN, PETER R · 2010 to 2020
$3.6M
National Institute of Allergy and Infectious Diseases R01AI089999NIAID NIH HHS R01 AI089999NIGMS NIH HHS P20 GM103466
6 · The paper itself

Abstract

Many of the 25 members of the selenoprotein family function as enzymes that utilize their selenocysteine (Sec) residues to catalyze redox-based reactions. However, some selenoproteins likely do not exert enzymatic activity by themselves and selenoprotein K (SELENOK) is one such selenoprotein family member that uses its Sec residue in an alternative manner. SELENOK is an endoplasmic reticulum (ER) transmembrane protein that has been shown to be important for ER stress and for calcium-dependent signaling. Molecular mechanisms for the latter have recently been elucidated using knockout mice and genetically manipulated cell lines. These studies have shown that SELENOK interacts with an enzyme in the ER membrane, DHHC6 (letters represent the amino acids aspartic acid, histidine, histidine, and cysteine in the catalytic domain), and the SELENOK/DHHC6 complex catalyzes the transfer of acyl groups such as palmitate to cysteine residues in target proteins, i.e., palmitoylation. One protein palmitoylated by SELENOK/DHHC6 is the calcium channel protein, the inositol 1,4,5-trisphosphate receptor (IP3R), which is acylated as a means for stabilizing the tetrameric calcium channel in the ER membrane. Factors that lower SELENOK levels or function impair IP3R-driven calcium flux. This role for SELENOK is important for the activation and proliferation of immune cells, and recently, a critical role for SELENOK in promoting calcium flux for the progression of melanoma has been demonstrated. This review provides a summary of these findings and their implications in terms of designing new therapeutic interventions that target SELENOK for treating cancers like melanoma.

Indexed as

Calcium SignalingEndoplasmic Reticulum StressNeoplasm ProteinsNeoplasmsSelenoproteinsAnimalsHumansMiceMice, KnockoutNeoplasm Proteinsselenoprotein K, humanselenoprotein K, mouseSelenoproteinsCalciumCancer therapyInositol 1,4,5-trisphosphate receptorPalmitoylationSeleniumSelenoprotein

Identifiers

PMID31187393
PMCPMC6801056
OpenAlexW2952812933

What Socratic holds

Textmetadata
LicenceTDM
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.