Evidence map›Paper›PMID 9819391›Full record

ArticleMolecular and cellular biology1998

ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src.

M T Brown, J Andrade, H Radhakrishna, J G Donaldson, J A Cooper, P A Randazzo

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 1 pooled it
5.4field-weighted citation impact, top 4% 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

103 citing papers in PubMed, 1 synthesis or guideline pooled it, 242 citations in OpenAlex.

  1. Pooled it
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  18. Cortactin in Lung Cell Function and Disease.International journal of molecular sciences · 2022
    Review
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43 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 3 countries.

M T BrownDivision of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA.
J Andrade
H Radhakrishna
J G Donaldson
J A Cooper
P A Randazzo
Cancer Institute (WIA) · INCape Town HVTN Immunology Laboratory / Hutchinson Centre Research Institute of South Africa · ZANational Heart Lung and Blood Institute · US

Funding

SRC FAMILY KINASES AND CELL GROWTH REGULATIONR37CA041072 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI COOPER, JONATHAN A. · 1999 to 2006
$3.3M
SRC FAMILY KINASES AND CELL GROWTH REGULATIONR01CA041072 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI COOPER, JONATHAN A · 1986 to 2011
$2.8M
SH3-BINDING PROTEINS, SIGNALING AND TRANSFORMATIONF32CA062598 · NCI · FRED HUTCHINSON CANCER RESEARCH CENTER · PI BROWN, MEGAN T · 1994 to 1996
–
NCI NIH HHS CA41072NCI NIH HHS CA62598NCI NIH HHS F32 CA062598NCI NIH HHS R01 CA041072NCI NIH HHS R37 CA041072
6 · The paper itself

Abstract

Membrane trafficking is regulated in part by small GTP-binding proteins of the ADP-ribosylation factor (Arf) family. Arf function depends on the controlled exchange and hydrolysis of GTP. We have purified and cloned two variants of a 130-kDa phosphatidylinositol 4, 5-biphosphate (PIP2)-dependent Arf1 GTPase-activating protein (GAP), which we call ASAP1a and ASAP1b. Both contain a pleckstrin homology (PH) domain, a zinc finger similar to that found in another Arf GAP, three ankyrin (ANK) repeats, a proline-rich region with alternative splicing and SH3 binding motifs, eight repeats of the sequence E/DLPPKP, and an SH3 domain. Together, the PH, zinc finger, and ANK repeat regions possess PIP2-dependent GAP activity on Arf1 and Arf5, less activity on Arf6, and no detectable activity on Arl2 in vitro. The cDNA for ASAP1 was independently identified in a screen for proteins that interact with the SH3 domain of the tyrosine kinase Src. ASAP1 associates in vitro with the SH3 domains of Src family members and with the Crk adapter protein. ASAP1 coprecipitates with Src from cell lysates and is phosphorylated on tyrosine residues in cells expressing activated Src. Both coimmunoprecipitation and tyrosine phosphorylation depend on the same proline-rich class II Src SH3 binding site required for in vitro association. By directly interacting with both Arfs and tyrosine kinases involved in regulating cell growth and cytoskeletal organization, ASAP1 could coordinate membrane remodeling events with these processes.

Indexed as

ADP-Ribosylation Factor 1ADP-Ribosylation FactorsAmino Acid SequenceAnimalsBrainCarrier ProteinsCattleEnzyme ActivationFluorescent Antibody TechniqueGTP-Binding ProteinsGTP PhosphohydrolasesMolecular Sequence DataPhosphatidylinositol 4,5-DiphosphatePhosphorylationPhosphotyrosineProtein BindingADP-Ribosylation Factor 1ADP-Ribosylation FactorsCarrier ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesPhosphatidylinositol 4,5-DiphosphatePhosphotyrosineProto-Oncogene ProteinsProto-Oncogene Proteins c-crkRecombinant Proteinssrc-Family Kinases

Identifiers

PMID9819391
PMCPMC109286
OpenAlexW2121634203

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.