Evidence map›Paper›PMID 12631729›Full record

ArticleMolecular biology of the cell2003

Obscurin is a ligand for small ankyrin 1 in skeletal muscle.

Aikaterini Kontrogianni-Konstantopoulos, Ellene M Jones, Damian B Van Rossum, Robert J Bloch

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 112 papers.

0numbers the graph read from it
0cells of the map it votes in
112citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

112 citing papers in PubMed, 186 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025
    Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Obscurin Maintains Myofiber Identity in Extraocular Muscles.Investigative ophthalmology & visual science · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Alterations in cytoskeletal and CaFrontiers in cardiovascular medicine · 2023
    Article
  15. Obscurin regulates ankyrin macromolecular complex formation.Journal of molecular and cellular cardiology · 2022
    Article
  16. Review
  17. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  18. Impaired Intracellular CaInternational journal of molecular sciences · 2022
    Article
  19. Obscurin: A multitasking giant in the fight against cancer.Biochimica et biophysica acta. Reviews on cancer · 2021
    Review
  20. Article

52 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

4 authors at 1 institution in 1 country.

Aikaterini Kontrogianni-KonstantopoulosDepartment of Physiology, University of Maryland, School of Medicine, Baltimore 21201, USA. akons001@umaryland.edu
Ellene M Jones
Damian B Van Rossum
Robert J Bloch
University of Maryland, Baltimore · US

Funding

SMALL ANKYRINS IN EXCITABLE CELLSR01HL064304 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI BLOCH, ROBERT J · 1999 to 2009
$2.3M
NHLBI NIH HHS R01 HL064304NHLBI NIH HHS R01 HL 64304NIAMS NIH HHS T32 AR 07293
6 · The paper itself

Abstract

The factors that organize the internal membranes of cells are still poorly understood. We have been addressing this question using striated muscle cells, which have regular arrays of membranes that associate with the contractile apparatus in stereotypic patterns. Here we examine links between contractile structures and the sarcoplasmic reticulum (SR) established by small ankyrin 1 (sAnk1), a approximately 17.5-kDa integral protein of network SR. We used yeast two-hybrid to identify obscurin, a giant Rho-GEF protein, as the major cytoplasmic ligand for sAnk1. The binding of obscurin to the cytoplasmic sequence of sAnk1 is mediated by a sequence of obscurin that is C-terminal to its last Ig-like domain. Binding was confirmed in two in vitro assays. In one, GST-obscurin, bound to glutathione-matrix, specifically adsorbed native sAnk1 from muscle homogenates. In the second, MBP-obscurin bound recombinant GST-sAnk1 in nitrocellulose blots. Kinetic studies using surface plasmon resonance yielded a K(D) = 130 nM. On subcellular fractionation, obscurin was concentrated in the myofibrillar fraction, consistent with its identification as sarcomeric protein. Nevertheless, obscurin, like sAnk1, concentrated around Z-disks and M-lines of striated muscle. Our findings suggest that obscurin binds sAnk1, and are the first to document a specific and direct interaction between proteins of the sarcomere and the SR.

Indexed as

Amino Acid SequenceAnimalsAnkyrinsBase SequenceCell FractionationGuanine Nucleotide Exchange FactorsHumansLigandsMolecular Sequence DataMuscle ProteinsMuscle, SkeletalMyocardiumProtein BindingProtein Serine-Threonine KinasesRatsRats, Sprague-DawleyANK1 protein, humanAnkyrinsGuanine Nucleotide Exchange FactorsLigandsMuscle ProteinsOBSCN protein, humanObscn protein, ratProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRho Guanine Nucleotide Exchange Factors

Identifiers

PMID12631729
PMCPMC151585
OpenAlexW2120618651

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.