Evidence map›Paper›PMID 17005911›Full record

ArticleMolecular biology of the cell2006

Not all secretory granules are created equal: Partitioning of soluble content proteins.

Jacqueline A Sobota, Francesco Ferraro, Nils Bäck, Betty A Eipper, Richard E Mains

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–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

32 citing papers in PubMed.

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  9. Polymers in the gut compress the colonic mucus hydrogel.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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.

Jacqueline A SobotaDepartment of Neuroscience, University of Connecticut Health Center, Farmington, CT 06030-3401, USA.
Francesco Ferraro
Nils Bäck
Betty A Eipper
Richard E Mains

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
SKELETAL, CRANOFACIAL AND ORAL BIOLOGY TRAIINING GRANTT32DE007302 · NIDCR · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI LURIE, ALAN GORDON · 1996 to 2010
$6.1M
Cell Biology of Bioactive Peptide SecretionR56DK032948 · NIDDK · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAINS, RICHARD E · 2008 to 2008
$303k
Peptidergic granules in trigeminal ganglion neuronsF30DE017094 · NIDCR · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI SOBOTA, JACQUELINE A · 2005 to 2008
$112k
CELL BIOLOGY OF BIOACTIVE PEPTIDE SECRETIONR37DK032948 · NIDDK · JOHNS HOPKINS UNIVERSITY · PI MAINS, RICHARD E · 1990 to 1998
–
NIDCR NIH HHS DE-007302NIDCR NIH HHS DE-017094NIDCR NIH HHS F30 DE017094NIDCR NIH HHS T32 DE007302NIDDK NIH HHS DK-32948NIDDK NIH HHS R01 DK032948NIDDK NIH HHS R56 DK032948
6 · The paper itself

Abstract

Secretory granules carrying fluorescent cargo proteins are widely used to study granule biogenesis, maturation, and regulated exocytosis. We fused the soluble secretory protein peptidylglycine alpha-hydroxylating monooxygenase (PHM) to green fluorescent protein (GFP) to study granule formation. When expressed in AtT-20 or GH3 cells, the PHM-GFP fusion protein partitioned from endogenous hormone (adrenocorticotropic hormone, growth hormone) into separate secretory granule pools. Both exogenous and endogenous granule proteins were stored and released in response to secretagogue. Importantly, we found that segregation of content proteins is not an artifact of overexpression nor peculiar to GFP-tagged proteins. Neither luminal acidification nor cholesterol-rich membrane microdomains play essential roles in soluble content protein segregation. Our data suggest that intrinsic biophysical properties of cargo proteins govern their differential sorting, with segregation occurring during the process of granule maturation. Proteins that can self-aggregate are likely to partition into separate granules, which can accommodate only a few thousand copies of any content protein; proteins that lack tertiary structure are more likely to distribute homogeneously into secretory granules. Therefore, a simple "self-aggregation default" theory may explain the little acknowledged, but commonly observed, tendency for both naturally occurring and exogenous content proteins to segregate from each other into distinct secretory granules.

Indexed as

Adrenocorticotropic HormoneBiological TransportCell LineCell MembraneCholesterolGreen Fluorescent ProteinsMixed Function OxygenasesModels, BiologicalMultienzyme ComplexesProteinsRecombinant Fusion ProteinsReproducibility of ResultsSecretory VesiclesSolubilityTransfectionVacuolesAdrenocorticotropic HormoneCholesterolGreen Fluorescent ProteinsMixed Function OxygenasesMultienzyme Complexespeptidylglycine monooxygenaseProteinsRecombinant Fusion Proteins

Identifiers

PMID17005911
PMCPMC1761688

What OpenQuestion holds

Textmetadata
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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.