Evidence map›Paper›PMID 9880325›Full record

ArticleMolecular biology of the cell1999

Sequences within the cytoplasmic domain of gp180/carboxypeptidase D mediate localization to the trans-Golgi network.

F J Eng, O Varlamov, L D Fricker

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 55 citations in OpenAlex.

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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 1 institution in 1 country.

F J EngDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
O Varlamov
L D Fricker
Albert Einstein College of Medicine · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
STRUCTURE/FUNCTION OF CARBOXYPEPTIDASE DR01DK051271 · NIDDK · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1996 to 2008
$2.7M
REGULATION OF NEUROPEPTIDE-PROCESSING ENZYMESK02DA000194 · NIDA · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1993 to 2002
$366k
NCI NIH HHS CA-13330NCI NIH HHS P30 CA013330NIDA NIH HHS DA-00194NIDDK NIH HHS DK-51271NIDDK NIH HHS R01 DK051271
6 · The paper itself

Abstract

Gp180, a duck protein that was proposed to be a cell surface receptor for duck hepatitis B virus, is the homolog of metallocarboxypeptidase D, a mammalian protein thought to function in the trans-Golgi network (TGN) in the processing of proteins that transit the secretory pathway. Both gp180 and mammalian metallocarboxypeptidase D are type I integral membrane proteins that contain a 58-residue cytosolic C-terminal tail that is highly conserved between duck and rat. To investigate the regions of the gp180 tail involved with TGN retention and intracellular trafficking, gp180 and various deletion and point mutations were expressed in the AtT-20 mouse pituitary corticotroph cell line. Full length gp180 is enriched in the TGN and also cycles to the cell surface. Truncation of the C-terminal 56 residues of the cytosolic tail eliminates the enrichment in the TGN and the retrieval from the cell surface. Truncation of 12-43 residues of the tail reduced retention in the TGN and greatly accelerated the turnover of the protein. In contrast, deletion of the C-terminal 45 residues, which truncates a potential YxxL-like sequence (FxxL), reduced the protein turnover and caused accumulation of the protein on the cell surface. A point mutation of the FxxL sequence to AxxL slowed internalization, showing that this element is important for retrieval from the cell surface. Mutation of a pair of casein kinase II sites within an acidic cluster showed that they are also important for trafficking. The present study demonstrates that multiple sequence elements within the cytoplasmic tail of gp180 participate in TGN localization.

Indexed as

ProteinsAmino Acid SequenceAnimalsBase SequenceBinding SitesBiological Transport, ActiveCarboxypeptidasesCell LineCell MembraneCycloheximideCytoplasmDNA, RecombinantDucksGolgi ApparatusHepatitis B Virus, DuckLysosomesCarboxypeptidasesCycloheximideDNA, RecombinantMembrane Glycoproteinsmetallocarboxypeptidase DProteinsReceptors, Virus

Identifiers

PMID9880325
PMCPMC25152
OpenAlexW2160266742

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.