Evidence map›Paper›PMID 35343388›Full record

ArticleJournal of biomolecular structure & dynamics2023

Parallel actin monomers in the 8S complex of actin-INF2.

Sanchaita Das, Zixin Zhang, Saichandra Kalvakota, Raul Soto, Martin L Phillips, Jonathan R Terman, Emil Reisler

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of biomolecular structure & dynamics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 49% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

7 authors at 2 institutions in 1 country.

Sanchaita DasDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
Zixin ZhangDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
Saichandra KalvakotaDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
Raul SotoDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
Martin L PhillipsDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
Jonathan R TermanDepartments of Neuroscience and Pharmacology, The University of Texas of Southwestern Medical Center, Dallas, TX, USA.
Emil ReislerDepartment of Chemistry and Biochemistry, University of California, Los Angeles, CA, USA.
University of California, Los Angeles · USSouthwestern Medical Center

Funding

Dynamic Events in Myosin and Actin and Their FunctionR01GM077190 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI REISLER, EMIL · 2006 to 2020
$6.2M
Molecular Mechanisms of Semaphorin/Plexin-mediated Cytoskeletal ReorganizationR01NS073968 · NINDS · UT SOUTHWESTERN MEDICAL CENTER · PI TERMAN, JONATHAN R · 2011 to 2022
$3.5M
NIGMS NIH HHS R01 GM077190NINDS NIH HHS R01 NS073968
6 · The paper itself

Abstract

Polymerization and depolymerization of actin play an essential role in eukaryotic cells. Actin exists in cells in both monomeric (G-actin) and filamentous (polymer, F-actin) forms. Actin binding proteins (ABPs) facilitate the transition between these two states, and their interactions with these two states of actin are critical for actin-based cellular processes. Rapid depolymerization of actin is assisted in the brain and/or other cells by its oxidation by the enzyme Mical (yielding Mox-actin), and/or by the binding of Inverted Formin 2 (INF2) - which can also accelerate filaments formation. At their stoichiometric molar ratio INF2 and actin yield the 8S complex (consisting of 4 actin monomers: 2 INF2 dimer molecules). Using biochemical and biophysical methods, we investigate the structural arrangement of actin in the 8S particles and the interaction of INF2 with actin and Mox-actin. To that end, we show 2 D class averages of 8S particles obtained by negative staining electron microscopy. We also show that: (i) 8S particles can seed rapid actin assembly; (ii) Mox-actin and INF2 form 8S particles at proteins ratios similar to those of unoxidized actin; (iii) chemical crosslinkings suggest that actin monomers are in a parallel orientation in the 8S particles of both actin and Mox-actin; and (iv) INF2 accelerates the disassembly of Mox-F-actin. Our results provide better understanding of actin's arrangement in the 8S particles formed during actin depolymerization and in the early polymerization stages of both actin and Mox-actin.Communicated by Ramaswamy H. Sarma.

Indexed as

ActinsMicrofilament ProteinsActin CytoskeletonForminsActinsForminsMicrofilament Proteins8S (8 Svedberg sedimentation coefficient units)Actinactin-INF2 8S particlesanalytical ultracentrifugationfluorescence assaysinverted formin 2 (INF2)Mical-oxidized actin (Mox-actin)protein crosslinkingrabbit skeletal actin

Identifiers

PMID35343388
PMCPMC10368088
OpenAlexW4221095087

What Socratic 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 Socratic graph.