Evidence map›Paper›PMID 23834433›Full record

ReviewAntioxidants & redox signaling2014

MICAL-family proteins: Complex regulators of the actin cytoskeleton.

Sai Srinivas Panapakkam Giridharan, Steve Caplan

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

66 citing papers in PubMed, 120 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. HIV-1 budding requires cortical actin disassembly by the oxidoreductase MICAL1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. tRNA modification enzyme-dependent redox homeostasis regulates synapse formation and memory.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. A Role for Second Messengers in Axodendritic Neuronal Polarity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Review
  17. Article
  18. Review
  19. Article
  20. Article

6 more citing papers are in PubMed but not listed here.

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.

Sai Srinivas Panapakkam GiridharanDepartment of Biochemistry and Molecular Biology, and the Pamela and Fred Buffett Cancer Center, University of Nebraska Medical Center , Omaha, Nebraska.
Steve Caplan
University of Nebraska Medical Center · US

Funding

Nebraska Center for Cellular SignalingP20GM103489 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI JOHNSON, KEITH R · 2012 to 2012
$2.0M
Regulation of EHD protein function by molecular partner interactionsR01GM087455 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI CAPLAN, STEVEN H, SORGEN, PAUL L · 2010 to 2013
$1.1M
NIGMS NIH HHS 5P20GM103489-10NIGMS NIH HHS P20 GM103489NIGMS NIH HHS R01 GM087455NIGMS NIH HHS R01GM087455
6 · The paper itself

Abstract

significanceThe molecules interacting with CasL (MICAL) family members participate in a multitude of activities, including axonal growth cone repulsion, membrane trafficking, apoptosis, and bristle development in flies. An interesting feature of MICAL proteins is the presence of an N-terminal flavo-mono-oxygenase domain. This mono-oxygenase domain generates redox potential with which MICALs can either oxidize proteins or produce reactive oxygen species (ROS). Actin is one such protein that is affected by MICAL function, leading to dramatic cytoskeletal rearrangements. This review describes the MICAL-family members, and discusses their mechanisms of actin-binding and regulation of actin cytoskeleton organization. RECENT ADVANCES: Recent studies show that MICALs directly induce oxidation of actin molecules, leading to actin depolymerization. ROS production by MICALs also causes oxidation of collapsin response mediator protein-2, a microtubule assembly promoter, which subsequently undergoes phosphorylation. CRITICAL ISSUES: MICAL proteins oxidize proteins through two mechanisms: either directly by oxidizing methionine residues or indirectly via the production of ROS. It remains unclear whether MICAL proteins employ both mechanisms or whether the activity of MICAL-family proteins might vary with different substrates. FUTURE DIRECTIONS: The identification of additional substrates oxidized by MICAL will shed new light on MICAL protein function. Additional directions include expanding studies toward the MICAL-like homologs that lack flavin adenine dinucleotide domains and oxidation activity.

Indexed as

ActinsAnimalsCytoskeletal ProteinsCytoskeletonHumansActinsCytoskeletal Proteins

Identifiers

PMID23834433
PMCPMC3993057
OpenAlexW2329437993

What OpenQuestion holds

Textmetadata
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.