Evidence map›Paper›PMID 25070890›Full record

ArticleThe Journal of biological chemistry2014

Crystal structure of the cGMP-dependent protein kinase II leucine zipper and Rab11b protein complex reveals molecular details of G-kinase-specific interactions.

Albert S Reger, Matthew P Yang, Shizuyo Koide-Yoshida, Elaine Guo, Shrenik Mehta, Keizo Yuasa, Alan Liu, Darren E Casteel, Choel Kim

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

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 22 citations in OpenAlex.

  1. Discovery of a Small Molecule with an Inhibitory Role for RAB11.International journal of molecular sciences · 2024
    Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Coiled-coils: The long and short of it.BioEssays : news and reviews in molecular, cellular and developmental biology · 2016
    Review
  8. Article
  9. CPT-cGMP Is A New Ligand of Epithelial Sodium Channels.International journal of biological sciences · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
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

9 authors at 4 institutions in 2 countries.

Albert S RegerFrom the Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030.
Matthew P Yangthe Departments of Biochemistry and.
Shizuyo Koide-Yoshidathe Department of Biological Science and Technology, University of Tokushima Graduate School, Tokushima 770-8506, Japan.
Elaine GuoChemistry, Rice University, Houston, Texas 77005.
Shrenik MehtaFrom the Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030.
Keizo Yuasathe Department of Biological Science and Technology, University of Tokushima Graduate School, Tokushima 770-8506, Japan.
Alan Liuthe Department of Medicine, University of California at San Diego, La Jolla, California 92093, and.
Darren E Casteelthe Department of Medicine, University of California at San Diego, La Jolla, California 92093, and.
Choel KimFrom the Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030, the Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030 ckim@bcm.edu.
Baylor College of Medicine · USRice University · USTokushima University · JPUniversity of California, San Diego · US

Funding

Targeting mechanisms of cGMP dependent protein kinases by peptide arrays and crysR01GM090161 · NIGMS · BAYLOR COLLEGE OF MEDICINE · PI KIM, CHOEL WOONG · 2010 to 2018
$2.9M
NIGMS NIH HHS R01 GM090161
6 · The paper itself

Abstract

cGMP-dependent protein kinase (PKG)-interacting proteins (GKIPs) mediate cellular targeting of PKG isoforms by interacting with their leucine zipper (LZ) domains. These interactions prevent aberrant signaling cross-talk between different PKG isotypes. To gain detailed insight into isotype-specific GKIP recognition by PKG, we analyzed the type II PKG leucine zipper domain and found that residues 40-83 dimerized and specifically interacted with Rab11b. Next, we determined a crystal structure of the PKG II LZ-Rab11b complex. The PKG II LZ domain presents a mostly nonpolar surface onto which Rab11b docks, through van der Waals interactions. Contact surfaces in Rab11b are found in switch I and II, interswitch, and the β1/N-terminal regions. This binding surface dramatically differs from that seen in the Rab11 family of interacting protein complex structures. Structural comparison with PKG Iα and Iβ LZs combined with mutagenic analysis reveals that GKIP recognition is mediated through surface charge interactions.

Indexed as

Crystallography, X-RayCyclic GMPCyclic GMP-Dependent Protein Kinase Type IIDimerizationEscherichia coliHeLa CellsHumansLeucine ZippersMultiprotein ComplexesProtein BindingProtein Interaction Domains and MotifsProtein Structure, Tertiaryrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsSignal TransductionCyclic GMPCyclic GMP-Dependent Protein Kinase Type IIMultiprotein Complexesrab11 GTP-Binding Proteinsrab GTP-Binding ProteinsCyclic GMP (cGMP)G-kinase-interacting Protein (GKIP)Protein Kinase G (PKG)Protein-Protein InteractionRabSecond MessengerSerine/Threonine Protein KinaseSignal TransductionType II cGMP-dependent Protein Kinase (PKG II)

Identifiers

PMID25070890
PMCPMC4162144
OpenAlexW1973511662

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.