Evidence map›Paper›PMID 11251076›Full record

ArticleMolecular biology of the cell2001

Signaling mediated by the cytosolic domain of peptidylglycine alpha-amidating monooxygenase.

M R Alam, T C Steveson, R C Johnson, N Bäck, B Abraham, R E Mains, B A Eipper

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

12 citing papers in PubMed, 32 citations in OpenAlex.

  1. Peptidylglycine α-amidating monooxygenase is required for atrial secretory granule formation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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  7. Signaling from the secretory granule to the nucleus: Uhmk1 and PAM.Molecular endocrinology (Baltimore, Md.) · 2010
    Article
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  11. Review
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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 1 institution in 1 country.

M R AlamDepartment of Neuroscience, University of Connecticut Health Center, Farmington, Connecticut 06030-3401, USA.
T C Steveson
R C Johnson
N Bäck
B Abraham
R E Mains
B A Eipper
UConn Health · US

Funding

CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR01DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, MAINS, RICHARD E · 1986 to 2019
$7.3M
Cell Biology of Bioactive Peptide SecretionR56DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAINS, RICHARD E · 2008 to 2008
$303k
CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR37DK032948 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MAINS, RICHARD E · 1990 to 1998
–
NIDDK NIH HHS DK-32948NIDDK NIH HHS R01 DK032948NIDDK NIH HHS R56 DK032948
6 · The paper itself

Abstract

The luminal domains of membrane peptidylglycine alpha-amidating monooxygenase (PAM) are essential for peptide alpha-amidation, and the cytosolic domain (CD) is essential for trafficking. Overexpression of membrane PAM in corticotrope tumor cells reorganizes the actin cytoskeleton, shifts endogenous adrenocorticotropic hormone (ACTH) from mature granules localized at the tips of processes to the TGN region, and blocks regulated secretion. PAM-CD interactor proteins include a protein kinase that phosphorylates PAM (P-CIP2) and Kalirin, a Rho family GDP/GTP exchange factor. We engineered a PAM protein unable to interact with either P-CIP2 or Kalirin (PAM-1/K919R), along with PAM proteins able to interact with Kalirin but not with P-CIP2. AtT-20 cells expressing PAM-1/K919R produce fully active membrane enzyme but still exhibit regulated secretion, with ACTH-containing granules localized to process tips. Immunoelectron microscopy demonstrates accumulation of PAM and ACTH in tubular structures at the trans side of the Golgi in AtT-20 cells expressing PAM-1 but not in AtT-20 cells expressing PAM-1/K919R. The ability of PAM to interact with P-CIP2 is critical to its ability to block exit from the Golgi and affect regulated secretion. Consistent with this, mutation of its P-CIP2 phosphorylation site alters the ability of PAM to affect regulated secretion.

Indexed as

Cyclic AMP-Dependent Protein KinasesMultienzyme ComplexesAdrenocorticotropic HormoneAnimalsBase SequenceBinding SitesCarrier ProteinsCell LineCytoplasmDNA PrimersGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsMicroscopy, ImmunoelectronMixed Function OxygenasesModels, BiologicalMutagenesis, Site-DirectedAdrenocorticotropic HormoneCarrier ProteinsCyclic AMP-Dependent Protein KinasesDNA PrimersGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsKalrn protein, ratMixed Function OxygenasesMultienzyme Complexespeptidylglycine monooxygenaseProtein Serine-Threonine KinasesProtein Sorting SignalsUhmk1 protein, rat

Identifiers

PMID11251076
PMCPMC30969
OpenAlexW2138769722

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.