Evidence map›Paper›PMID 15767667›Full record

ArticleMolecular and cellular biology2005

Kinase activation through dimerization by human SH2-B.

Masahiro Nishi, Eric D Werner, Byung-Chul Oh, J Daniel Frantz, Sirano Dhe-Paganon, Lone Hansen, Jongsoon Lee, Steven E Shoelson

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

31 citing papers in PubMed, 59 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Masahiro NishiJoslin Diabetes Center, One Joslin Place, Boston, MA 02215, USA.
Eric D Werner
Byung-Chul Oh
J Daniel Frantz
Sirano Dhe-Paganon
Lone Hansen
Jongsoon Lee
Steven E Shoelson
Joslin Diabetes Center · US

Funding

SPECIAL ASSAY COREP30DK036836 · NIDDK · JOSLIN DIABETES CENTER · PI ROHIT N. KULKARNI · 1986 to 2026
$50.5M
POTENTIAL CAUSE &MOLECULAR TARGET OF INSULIN RESISTANCR01DK045943 · NIDDK · JOSLIN DIABETES CENTER · PI SHOELSON, STEVEN E · 1996 to 2009
$3.1M
STRUCTURE OF IRS PROTEINS IN INSULIN RESISTANCER01DK043123 · NIDDK · JOSLIN DIABETES CENTER · PI SHOELSON, STEVEN E · 1992 to 2008
$2.7M
TREATING INSULIN RESISTANCE AND DIABETESF32DK009908 · NIDDK · JOSLIN DIABETES CENTER · PI WERNER, ERIC D · 1999 to 2001
$80k
LYMPHOID TISSUE-RESTRICTED ISOFORM OF GRB2F32DK009393 · NIDDK · JOSLIN DIABETES CENTER · PI FRANTZ, JAMES D · 1996 to 1998
–
NIDDK NIH HHS DK09393NIDDK NIH HHS DK09908NIDDK NIH HHS DK36836NIDDK NIH HHS DK43123NIDDK NIH HHS DK45943NIDDK NIH HHS F32 DK009393NIDDK NIH HHS F32 DK009908NIDDK NIH HHS P30 DK036836NIDDK NIH HHS R01 DK043123NIDDK NIH HHS R01 DK045943
6 · The paper itself

Abstract

The isoforms of SH2-B, APS, and Lnk form a family of signaling proteins that have been described as activators, mediators, or inhibitors of cytokine and growth factor signaling. We now show that the three alternatively spliced isoforms of human SH2-B readily homodimerize in yeast two-hybrid and cellular transfections assays, and this is mediated specifically by a unique domain in its amino terminus. Consistent with previous reports, we further show that the SH2 domains of SH2-B and APS bind JAK2 at Tyr813. These findings suggested a model in which two molecules of SH2-B or APS homodimerize with their SH2 domains bound to two JAK2 molecules, creating heterotetrameric JAK2-(SH2-B)2-JAK2 or JAK2-(APS)2-JAK2 complexes. We further show that APS and SH2-B isoforms heterodimerize. At lower levels of SH2-B or APS expression, dimerization approximates two JAK2 molecules to induce transactivation. At higher relative concentrations of SH2-B or APS, kinase activation is blocked. SH2-B or APS homodimerization and SH2-B/APS heterodimerization thus provide direct mechanisms for activating and inhibiting JAK2 and other kinases from the inside of the cell and for potentiating or attenuating cytokine and growth factor receptor signaling when ligands are present.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCarrier ProteinsCell LineCloning, MolecularDimerizationDNA-Binding ProteinsEnzyme ActivationHumansJanus Kinase 2MiceMilk ProteinsModels, MolecularMolecular Sequence DataPhosphorylationAdaptor Proteins, Signal Transducingadenylylsulfate kinaseCarrier ProteinsDNA-Binding ProteinsJAK2 protein, humanJak2 protein, mouseJanus Kinase 2Milk ProteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineProtein IsoformsProtein KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsSH2B1 protein, humanSTAT5 Transcription FactorTrans-Activators

Identifiers

PMID15767667
PMCPMC1061652
OpenAlexW2101323755

What Socratic 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 Socratic graph.