Evidence map›Paper›PMID 33132189›Full record

ArticleJournal of structural biology2020

Insight into human Miro1/2 domain organization based on the structure of its N-terminal GTPase.

Kyle P Smith, Pamela J Focia, Srinivas Chakravarthy, Eric C Landahl, Julian L Klosowiak, Sarah E Rice, Douglas M Freymann

Open access · greenAbstract read
In one paragraph

Article in Journal of structural biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  15. Miro proteins and their role in mitochondrial transfer in cancer and beyond.Frontiers in cell and developmental biology · 2022
    Review
  16. Review
  17. Review
  18. The Emerging Role ofFrontiers in neurology · 2020
    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 3 institutions in 1 country.

Kyle P SmithDepartment of Cell & Molecular Biology, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA. Electronic address: kyle.smith.phd@gmail.com.
Pamela J FociaDepartment of Biochemistry & Molecular Genetics, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.
Srinivas ChakravarthyBiophysics Collaborative Access Team, Advanced Photon Source, Argonne National Laboratory, Bldg. 435B/Sector 18, 9700 S. Cass Avenue, Argonne, IL 60439, USA.
Eric C LandahlDepartment of Physics, DePaul University, Chicago, IL 60614, USA.
Julian L KlosowiakDepartment of Cell & Molecular Biology, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.
Sarah E RiceDepartment of Physical Therapy and Human Movement Sciences, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611, USA.
Douglas M FreymannDepartment of Biochemistry & Molecular Genetics, Feinberg School of Medicine, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA. Electronic address: freymann@northwestern.edu.
Northwestern University · USArgonne National Laboratory · USDePaul University · US

Funding

Tumor Environment and Metastasis (TEAM) Research ProgramP30CA060553 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI LEONIDAS C. PLATANIAS · 1993 to 2026
$153.9M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Src kinase phosphoregulation of the human mitotic kinesin, Eg5R01GM107209 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI RICE, SARAH E. · 2013 to 2016
$1.4M
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
$529k
NCI NIH HHS P30 CA060553NIGMS NIH HHS P41 GM103622NIGMS NIH HHS R01 GM107209NIGMS NIH HHS T32 GM008382NIH HHS S10 OD018090
6 · The paper itself

Abstract

Dysfunction in mitochondrial dynamics is believed to contribute to a host of neurological disorders and has recently been implicated in cancer metastasis. The outer mitochondrial membrane adapter protein Miro functions in the regulation of mitochondrial mobility and degradation, however, the structural basis for its roles in mitochondrial regulation remain unknown. Here, we report a 1.7Å crystal structure of N-terminal GTPase domain (nGTPase) of human Miro1 bound unexpectedly to GTP, thereby revealing a non-catalytic configuration of the putative GTPase active site. We identify two conserved surfaces of the nGTPase, the "SELFYY" and "ITIP" motifs, that are potentially positioned to mediate dimerization or interaction with binding partners. Additionally, we report small angle X-ray scattering (SAXS) data obtained from the intact soluble HsMiro1 and its paralog HsMiro2. Taken together, the data allow modeling of a crescent-shaped assembly of the soluble domain of HsMiro1/2. PDB RSEFERENCE: Crystal structure of the human Miro1 N-terminal GTPase bound to GTP, 6D71.

Indexed as

Amino Acid SequenceGTP PhosphohydrolasesHumansMitochondriaMitochondrial MembranesMitochondrial ProteinsProtein Domainsrho GTP-Binding ProteinsScattering, Small AngleX-Ray DiffractionGTP PhosphohydrolasesMitochondrial Proteinsrho GTP-Binding ProteinsRHOT1 protein, humanRHOT2 protein, humanCrystal structureGem1pGTP-binding proteinMiroMitochondrial dynamicsRhoT

Identifiers

PMID33132189
PMCPMC7744357
OpenAlexW3094062383

What OpenQuestion 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 OpenQuestion graph.