Evidence map›Paper›PMID 19635792›Full record

ArticleThe Journal of biological chemistry2009

Secretory granule to the nucleus: role of a multiply phosphorylated intrinsically unstructured domain.

Chitra Rajagopal, Kathryn L Stone, Victor P Francone, Richard E Mains, Betty A Eipper

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Review
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  5. Identifying roles for peptidergic signaling in mice.Proceedings of the National Academy of Sciences of the United States of America · 2019
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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

5 authors at 2 institutions in 1 country.

Chitra RajagopalDepartment of Molecular, Microbial, and Structural Biology, University of Connecticut Health Center, Farmington, Connecticut 06030, USA.
Kathryn L Stone
Victor P Francone
Richard E Mains
Betty A Eipper
UConn Health · USYale University · US

Funding

YALE UNIVERSITY CLINICAL AND TRANSLATIONAL SCIENCE AWARD PROGRAMUL1RR024139 · NCRR · YALE UNIVERSITY · PI SHERWIN, ROBERT S · 2006 to 2011
$56.8M
Yale/NIDA Neuroproteomics Research CenterP30DA018343 · NIDA · YALE UNIVERSITY · PI Marina R Picciotto · 2004 to 2026
$37.1M
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR01DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH ANNE, KING, STEPHEN M · 1986 to 2017
$6.4M
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR37DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH A · 1989 to 2004
$2.8M
LTQ-Orbitrap Mass Spectrometer for Yale University Keck LaboratoryS10RR024617 · NCRR · YALE UNIVERSITY · PI GULCICEK, EROL E · 2008 to 2008
$500k
BIOCHEMISTRY AND PHYSIOLOGY OF PEPTIDE AMIDATIONR56DK032949 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI EIPPER, ELIZABETH A · 2005 to 2005
$104k
NCRR NIH HHS 1S10RR024617NCRR NIH HHS S10 RR024617NCRR NIH HHS UL1 RR024139NIDA NIH HHS P30 DA018343NIDDK NIH HHS DK32949NIDDK NIH HHS R01 DK032949NIDDK NIH HHS R37 DK032949NIDDK NIH HHS R56 DK032949
6 · The paper itself

Abstract

Intrinsically unstructured domains occur in one-third of all proteins and are characterized by conformational flexibility, protease sensitivity, and the occurrence of multiple phosphorylation. They provide large interfaces for diverse protein-protein interactions. Peptidylglycine alpha-amidating monooxygenase (PAM), an enzyme essential for neuropeptide biosynthesis, is a secretory granule membrane protein. As one of the few proteins spanning the granule membrane, PAM is a candidate to relay information about the status of the granule pool and conditions in the granule lumen. Here, we show that the PAM cytosolic domain is unstructured. Mass spectroscopy and two-dimensional gel electrophoresis demonstrated phosphorylation at 10-12 sites in the cytosolic domain. Stimulation of exocytosis resulted in coupled phosphorylation and dephosphorylation of specific sites and in the endoproteolytic release of a soluble, proteasome-sensitive cytosolic domain fragment. Analysis of granule-rich tissues, such as pituitary and heart, showed that a similar fragment was generated endogenously and translocated to the nucleus. This multiply phosphorylated unstructured domain may act as a signaling molecule that relays information from secretory granules to both cytosol and nucleus.

Indexed as

Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingCell LineCell NucleusExocytosisHumansMixed Function OxygenasesPhosphorylationProtein Structure, TertiarySecretory VesiclesUbiquitin-Protein LigasesAdaptor Proteins, Signal TransducingMixed Function OxygenasesMYCBP2 protein, humanUbiquitin-Protein Ligases

Identifiers

PMID19635792
PMCPMC2757974
OpenAlexW2088425060

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.