Evidence map›Paper›PMID 11879186›Full record

ArticleThe Biochemical journal2002

The beta-appendages of the four adaptor-protein (AP) complexes: structure and binding properties, and identification of sorting nexin 9 as an accessory protein to AP-2.

Richard Lundmark, Sven R Carlsson

Abstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
–field-weighted citation impact
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

20 citing papers in PubMed, 1 synthesis or guideline pooled it.

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  18. Cell biology of membrane trafficking in human disease.International review of cytology · 2006
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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

2 authors.

Richard LundmarkDepartment of Medical Biochemistry and Biophysics, Umeå University, S-901 87 Umeå, Sweden.
Sven R Carlsson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adaptor protein (AP) complexes are essential components for the formation of coated vesicles and the recognition of cargo proteins for intracellular transport. Each AP complex exposes two appendage domains with that function to bind regulatory accessory proteins in the cytosol. Secondary structure predictions, sequence alignments and CD spectroscopy were used to relate the beta-appendages of all human AP complexes to the previously published crystal structure of AP-2. The results suggested that the beta-appendages of AP-1, AP-2 and AP-3 have similar structures, consisting of two subdomains, whereas that of AP-4 lacks the inner subdomain. Pull-down and overlay assays showed partial overlap in the binding specificities of the beta-appendages of AP-1 and AP-2, whereas the corresponding domain of AP-3 displayed a unique binding pattern. That AP-4 may have a truncated, non-functional domain was indicated by its apparent inability to bind any proteins from cytosol. Of several novel beta-appendage-binding proteins detected, one that had affinity exclusively for AP-2 was identified as sorting nexin 9 (SNX9). SNX9, which contains a phox and an Src homology 3 domain, was found in large complexes and was at least partially associated with AP-2 in the cytosol. SNX9 may function to assist AP-2 in its role at the plasma membrane.

Indexed as

Adaptor Protein Complex 3Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex delta SubunitsAmino Acid SequenceBinding SitesCarrier ProteinsCell MembraneCircular DichroismConserved SequenceCytosolGlutathione TransferaseHumansMembrane ProteinsMolecular Sequence DataProtein ConformationProtein Structure, SecondaryAdaptor Protein Complex 3Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex delta SubunitsAP3D1 protein, humanCarrier ProteinsGlutathione TransferaseMembrane ProteinsRecombinant Fusion ProteinsSNX9 protein, humanSorting NexinsTranscription Factor AP-1Transcription FactorsVesicular Transport Proteins

Identifiers

PMID11879186
PMCPMC1222423

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.