Evidence map›Paper›PMID 10359609›Full record

ArticleMolecular biology of the cell1999

The PDZ domain of the LIM protein enigma binds to beta-tropomyosin.

P M Guy, D A Kenny, G N Gill

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

39 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. The unexpected versatility of ALP/Enigma family proteins.Frontiers in cell and developmental biology · 2022
    Review
  8. Article
  9. Article
  10. Overview of the Muscle Cytoskeleton.Comprehensive Physiology · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. The sarcomeric Z-disc and Z-discopathies.Journal of biomedicine & biotechnology · 2011
    Review
  18. Article
  19. Article
  20. ALP/Enigma PDZ-LIM domain proteins in the heart.Journal of molecular cell biology · 2010
    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

3 authors at 1 institution in 1 country.

P M GuyDepartment of Medicine, University of California at San Diego, La Jolla, California 92093-0650, USA.
D A Kenny
G N Gill
University of California San Diego · US

Funding

VESICULAR TRAFFICKING OF THE EGF RECEPTORP01CA058689 · NCI · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI FARQUHAR, MARILYN GIST · 1993 to 2002
$5.0M
Translational Cardiovascular Science and MedicineT32HL007770 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI EVANS, RONALD M. · 1993 to 2007
$2.8M
BIOLOGICAL FUNCTIONS OF LIM DOMAIN CONTAINING PROTEINSF32DK009320 · NIDDK · UNIVERSITY OF CALIFORNIA SAN DIEGO · PI GUY, PAMELA M · 1995 to 1997
–
NCI NIH HHS 5PO 1 CA58689NHLBI NIH HHS T32 HL007770NHLBI NIH HHS T32HL-07770NIDDK NIH HHS DK-09320NIDDK NIH HHS F32 DK009320
6 · The paper itself

Abstract

PDZ and LIM domains are modular protein interaction motifs present in proteins with diverse functions. Enigma is representative of a family of proteins composed of a series of conserved PDZ and LIM domains. The LIM domains of Enigma and its most related family member, Enigma homology protein, bind to protein kinases, whereas the PDZ domains of Enigma and family member actin-associated LIM protein bind to actin filaments. Enigma localizes to actin filaments in fibroblasts via its PDZ domain, and actin-associated LIM protein binds to and colocalizes with the actin-binding protein alpha-actinin-2 at Z lines in skeletal muscle. We show that Enigma is present at the Z line in skeletal muscle and that the PDZ domain of Enigma binds to a skeletal muscle target, the actin-binding protein tropomyosin (skeletal beta-TM). The interaction between Enigma and skeletal beta-TM was specific for the PDZ domain of Enigma, was abolished by mutations in the PDZ domain, and required the PDZ-binding consensus sequence (Thr-Ser-Leu) at the extreme carboxyl terminus of skeletal beta-TM. Enigma interacted with isoforms of tropomyosin expressed in C2C12 myotubes and formed an immunoprecipitable complex with skeletal beta-TM in transfected cells. The association of Enigma with skeletal beta-TM suggests a role for Enigma as an adapter protein that directs LIM-binding proteins to actin filaments of muscle cells.

Indexed as

Intracellular Signaling Peptides and ProteinsActinsAmino Acid SequenceAnimalsBinding SitesCarrier ProteinsCell LineCytoskeletal ProteinsGene Expression Regulation, DevelopmentalLIM Domain ProteinsMiceMolecular Sequence DataMuscle, SkeletalMutationPeptide FragmentsPrecipitin TestsActinsCarrier ProteinsCipp protein, mouseCytoskeletal ProteinsIntracellular Signaling Peptides and ProteinsLIM Domain ProteinsPdlim7 protein, mousePeptide FragmentsProtein IsoformsTropomyosin

Identifiers

PMID10359609
PMCPMC25398
OpenAlexW2169012342

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.