Evidence map›Paper›PMID 11607843›Full record

ReviewOncogene2001

The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity.

J M Baisden, Y Qian, H M Zot, D C Flynn

Open access · bronzeAbstract readReview
PubMed Publisher
In one paragraph

Review in Oncogene, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

40 citing papers in PubMed, 68 citations in OpenAlex.

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  19. AFAP1-AS1, a long noncoding RNA upregulated in lung cancer and promotes invasion and metastasis.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
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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

4 authors at 2 institutions in 1 country.

J M BaisdenDepartment Microbiology & Immunology, Mary Babb Randolph Cancer Center, West Virginia University, Morgantown, West Virginia, WV 26506-9300 USA.
Y Qian
H M Zot
D C Flynn
West Virginia University · USEastern Michigan University · US

Funding

AFAP-110 regulates signals that affect F-actinR01CA060731 · NCI · WEST VIRGINIA UNIVERSITY · PI HOLT, JEFFREY T · 1999 to 2012
$3.3M
PP60SRC BINDING PROTEIN AFAP-110R29CA060731 · NCI · WEST VIRGINIA UNIVERSITY · PI FLYNN, DANIEL · 1994 to 1998
–
NCI NIH HHS CA60731
6 · The paper itself

Abstract

The actin filament-associated protein of 110 kDa (AFAP-110) was first identified as an SH3/SH2 binding partner for the nonreceptor tyrosine kinase, Src. Subsequent data have demonstrated that AFAP-110 can interact with other Src family members. AFAP-110 contains additional protein binding modules including two pleckstrin homology domains, a leucine zipper motif and a target sequence for serine/threonine phosphorylation. AFAP-110 interacts with actin filaments directly via a carboxy terminal actin-binding domain. Thus AFAP-110 may function as an adaptor protein by linking Src family members and/or other signaling proteins to actin filaments. AFAP-110 also has an intrinsic capability to alter actin filament integrity that can be revealed upon conformational changes associated with phosphorylation or mutagenesis. Recent data has indicated that AFAP-110 may also serve to activate cSrc in response to this conformational change as well. Thus, AFAP-110 may function in several ways by (1) acting as an adaptor protein that links signaling molecules to actin filaments, (2) serving as a platform for the construction of larger signaling complexes, (3) serving as an activator of Src family kinases in response to cellular signals that alter its conformation and (4) directly effecting actin filament organization as an actin filament cross-linking protein. Here, we will review the structure and function of AFAP-110 as well as potential binding partners and effectors of AFAP-110's ability to alter actin filament integrity.

Indexed as

ActinsAmino Acid MotifsAmino Acid SequenceAnimalsHumansMicrofilament ProteinsModels, BiologicalMolecular Sequence DataPhospholipidsPhosphoproteinsPhosphorylationProtein BindingProtein Kinase CProtein Structure, TertiarySequence Homology, Amino AcidSignal TransductionActinsAFAP 110Microfilament ProteinsPhospholipidsPhosphoproteinsProtein Kinase CTyrosine

Identifiers

PMID11607843
OpenAlexW2332783311

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.