Evidence map›Paper›PMID 9412467›Full record

ArticleThe Journal of cell biology1997

Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway.

G Liu, L Thomas, R A Warren, C A Enns, C C Cunningham, J H Hartwig, G Thomas

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

58 citing papers in PubMed, 141 citations in OpenAlex.

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  14. Brefeldin A-inhibited guanine exchange factor 2 regulates filamin A phosphorylation and neuronal migration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
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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

7 authors at 4 institutions in 1 country.

G LiuVollum Institute, Oregon Health Sciences University, Portland, Oregon 97201, USA.
L Thomas
R A Warren
C A Enns
C C Cunningham
J H Hartwig
G Thomas
Oregon Health & Science University · USVollum Institute · USBrigham and Women's Hospital · USHarvard University · US

Funding

MULTIDISCIPLINARY TRAINING IN NEUROENDOCRINOLOGYT32DK007680 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI GOODMAN, RICHARD H. · 1991 to 2015
$6.8M
Role of PACS proteins in polycystin-2 trafficking and ADPKDR01DK037274 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI THOMAS, GARY · 1986 to 2010
$3.3M
TRAINING IN ENDOCRINOLOGY, DIABETES, NUTRITIONT32DK007674 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI KLEIN, ROBERT FREDERICK · 1993 to 2013
$3.1M
STRUCTURE/FUNCTION OF TRANSFERRIN RECEPTORR01DK040608 · NIDDK · SYRACUSE UNIVERSITY AT SYRACUSE · PI ENNS, CAROLINE · 1989 to 2002
$742k
ROLE OF HUMAN FURIN PROCESSING ENDOPROTEASER01DK044629 · NIDDK · OREGON HEALTH AND SCIENCE UNIVERSITY · PI THOMAS, GARY · 1992 to 2000
$182k
IDENTIFYING THE ROLE OF ABP-280 IN FURIN TRAFFICKINGF32DK009394 · NIDDK · OREGON HEALTH AND SCIENCE UNIVERSITY · PI LIU, GSEPING · 1997 to 1998
–
NIDDK NIH HHS DK-37274NIDDK NIH HHS DK-40608NIDDK NIH HHS DK-44629NIDDK NIH HHS F32 DK009394NIDDK NIH HHS R01 DK037274NIDDK NIH HHS T32 DK007674NIDDK NIH HHS T32 DK007680
6 · The paper itself

Abstract

Furin catalyzes the proteolytic maturation of many proproteins within the trans-Golgi network (TGN)/endosomal system. Furin's cytosolic domain (cd) directs both the compartmentalization to and transit between its manifold processing compartments (i.e., TGN/biosynthetic pathway, cell surface, and endosomes). Here we report the identification of the first furin cd sorting protein, ABP-280 (nonmuscle filamin), an actin gelation protein. The furin cd was used as bait in a yeast two-hybrid screen to identify ABP-280 as a furin-binding protein. Binding analyses in vitro and coimmunoprecipitation studies in vivo showed that furin and ABP-280 interact directly and that ABP-280 tethers furin molecules to the cell surface. Quantitative analysis of both ABP-280-deficient and genetically replete cells showed that ABP-280 modulates the rate of internalization of furin but not of the transferrin receptor, a cycling receptor. However, although ABP-280 directs the rate of furin internalization, the efficiency of sorting of the endoprotease from the cell surface to early endosomes is independent of expression of ABP-280. By contrast, efficient sorting of furin from early endosomes to the TGN requires expression of ABP-280. In addition, ABP-280 is also required for the correct localization of late endosomes (dextran bead uptake) and lysosomes (LAMP-1 staining), demonstrating a pleiotropic role for this actin binding protein in the organization of cellular compartments and directing protein traffic. Finally, and consistent with the trafficking studies on furin, we showed that ABP-280 modulates the processing of furin substrates in the endocytic but not the biosynthetic pathways. The novel roles of ABP-280 and the cytoskeleton in the sorting of furin in the TGN/ endosomal system and the formation of proprotein processing compartments are discussed.

Indexed as

Protein Processing, Post-TranslationalAmino Acid SequenceAnimalsBase SequenceCarrier ProteinsCell CompartmentationCell LineCell MembraneChlorocebus aethiopsContractile ProteinsEndocytosisEndosomesFilaminsFurinHumansLysosomesCarrier ProteinsContractile ProteinsFilaminsFurinMicrofilament ProteinsProtein PrecursorsReceptors, TransferrinSubtilisins

Identifiers

PMID9412467
PMCPMC1424222
OpenAlexW2046390241

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.