Biophysical characterization of SARAH domain-mediated multimerization of Hippo pathway complexes in

Animals Drosophila Proteins / chemistry Drosophila melanogaster Intracellular Signaling Peptides and Proteins / chemistry Models, Molecular Protein Domains Protein Multimerization Protein Serine-Threonine Kinases / chemistry
Hippo pathway MST2 (mammalian sterile 20-like kinase 2) SARAH domain Salvador (sav) Sav/RassF/Hpo domain cell proliferation cell signaling protein-protein interaction structure-function

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
01 05 2020
Historique:
received: 16 01 2020
revised: 23 03 2020
pubmed: 28 3 2020
medline: 29 12 2020
entrez: 28 3 2020
Statut: ppublish

Résumé

Hippo pathway signaling limits cell growth and proliferation and maintains the stem-cell niche. These cellular events result from the coordinated activity of a core kinase cassette that is regulated, in part, by interactions involving Hippo, Salvador, and dRassF. These interactions are mediated by a conserved coiled-coil domain, termed SARAH, in each of these proteins. SARAH domain-mediated homodimerization of Hippo kinase leads to autophosphorylation and activation. Paradoxically, SARAH domain-mediated heterodimerization between Hippo and Salvador enhances Hippo kinase activity in cells, whereas complex formation with dRassF inhibits it. To better understand the mechanism by which each complex distinctly modulates Hippo kinase and pathway activity, here we biophysically characterized the entire suite of SARAH domain-mediated complexes. We purified the three SARAH domains from

Identifiants

DOI: 10.1074/jbc.RA120.012679 PMID: 32213597 PMC: PMC7196646
pubmed: 32213597
pii: S0021-9258(17)48246-9
doi: 10.1074/jbc.RA120.012679
pmc: PMC7196646
pii:
doi:

Substances chimiques

Drosophila Proteins 0
Intracellular Signaling Peptides and Proteins 0
Protein Serine-Threonine Kinases EC 2.7.11.1
hpo protein, Drosophila EC 2.7.11.1

Banques de données

PDB
['6BN1']

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Langues

eng

Sous-ensembles de citation

IM

Pagination

6202-6213

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM134000
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009110
Pays : United States
Organisme : NIGMS NIH HHS
ID : P20 GM103474
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007445
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM080189
Pays : United States

Informations de copyright

© 2020 Cairns et al.

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Auteurs

Leah Cairns (L)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, 20215.

Angela Patterson (A)

Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, 59717.

Kyler A Weingartner (KA)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, 20215.

T J Koehler (TJ)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, 20215.

Daniel R DeAngelis (DR)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, 20215.

Katherine W Tripp (KW)

The T. C. Jenkins Department of Biophysics, Krieger School of Arts and Sciences, Johns Hopkins University, Baltimore, Maryland, 201218.

Brian Bothner (B)

Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana, 59717.

Jennifer M Kavran (JM)

Department of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, Maryland, 20215; Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland 20215; Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, Maryland, 20215. Electronic address: jkavran@jhu.edu.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Biophysical characterization of SARAH...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines d'arthropode › Protéines d'insecte › Protéines de Drosophila › Biophysical characterization of SARAH...
questionsmedicales.fr › Eucaryotes › Animaux › Invertébrés › Arthropodes › Insectes › Pterygota › Neoptera › Holometabola › Diptera › Drosophilidae › Drosophila › Drosophila melanogaster › Biophysical characterization of SARAH...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Biophysical characterization of SARAH...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Biophysical characterization of SARAH...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Biophysical characterization of SARAH...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Multimérisation de protéines › Biophysical characterization of SARAH...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Biophysical characterization of SARAH...