Evidence map›Paper›PMID 15557335›Full record

ArticleThe Journal of biological chemistry2005

Src phosphorylation of Alix/AIP1 modulates its interaction with binding partners and antagonizes its activities.

Mirko Schmidt, Ivan Dikic, Oliver Bögler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 69 citations in OpenAlex.

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  11. Syntenin mediates SRC function in exosomal cell-to-cell communication.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

3 authors at 2 institutions in 2 countries.

Mirko SchmidtWilliam and Karen Davidson Laboratory of Brain Tumor Biology, Hermelin Brain Tumor Center, Department of Neurosurgery, Henry Ford Hospital, Detroit, Michigan 48202, USA.
Ivan Dikic
Oliver Bögler
Henry Ford Hospital · USGoethe University Frankfurt · DE

Funding

Regulation of RTKs by the SETA/CIN85 Complex in GliomaR01CA108500 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI BOGLER, OLIVER · 2004 to 2008
$1.1M
APOPTOSIS AND A NEW ADAPTER MOLECULE PATHWAY IN GLIOMAR01CA084109 · NCI · HENRY FORD HEALTH SYSTEM · PI BOGLER, OLIVER · 2001 to 2004
$897k
NCI NIH HHS CA-R01-108500NCI NIH HHS CA-R01-84109NCI NIH HHS R01 CA084109NCI NIH HHS R01 CA108500
6 · The paper itself

Abstract

Alix/AIP1 is an adaptor protein involved in regulating the function of receptor and cytoskeleton-associated tyrosine kinases. Here, we investigated its interaction with and regulation by Src. Tyr319 of Alix bound the isolated Src homology-2 (SH2) domain and was necessary for interaction with intact Src. A proline-rich region in the C terminus of Alix bound the Src SH3 domain, but this interaction was dependent on the release of the Src SH2 domain from its Src internal ligand either by interaction with Alix Tyr319 or by mutation of Src Tyr527. Src phosphorylated Alix at a C-terminal region rich in tyrosines, an activity that was stimulated by the presence of the Alix binding partner SETA/CIN85. Phosphorylation of Alix by Src caused it to translocate from the membrane and cytoskeleton to the cytoplasm and reduced its interaction with binding partners SETA/CIN85, epidermal growth factor receptor, and Pyk2. As a consequence of this, Src antagonized the negative regulation of receptor tyrosine kinase internalization and cell adhesion by Alix. We propose a model whereby Src antagonizes the effects of Alix by phosphorylation of its C terminus, leading to the disruption of interactions with target proteins.

Indexed as

AnimalsAstrocytesCalcium-Binding ProteinsCarrier ProteinsCell LineCell MembraneCerebral CortexCytoplasmCytoskeletonPhosphorylationProtein BindingProtein Structure, TertiaryRatssrc-Family Kinasessrc Homology DomainsTyrosineCalcium-Binding ProteinsCarrier ProteinsPdcd6ip protein, ratsrc-Family KinasesTyrosine

Identifiers

PMID15557335
PMCPMC1180480
OpenAlexW2020379551

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.