Evidence map›Paper›PMID 22170066›Full record

ArticleThe Journal of biological chemistry2012

Cytosolic carboxypeptidase 1 is involved in processing α- and β-tubulin.

Iryna Berezniuk, Hang T Vu, Peter J Lyons, Juan J Sironi, Hui Xiao, Berta Burd, Mitsutoshi Setou, Ruth H Angeletti, Koji Ikegami, Lloyd D Fricker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

61 citing papers in PubMed, 103 citations in OpenAlex.

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1 more citing papers are in PubMed but not listed here.

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

10 authors at 2 institutions in 2 countries.

Iryna BerezniukDepartment of Neuroscience, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Hang T Vu
Peter J Lyons
Juan J Sironi
Hui Xiao
Berta Burd
Mitsutoshi Setou
Ruth H Angeletti
Koji Ikegami
Lloyd D Fricker
Albert Einstein College of Medicine · USHamamatsu University School of Medicine · JP

Funding

REGULATION OF ENKEPHALIN CONVERTASE--CARBOXYPEPTIDASE ER01DA004494 · NIDA · YESHIVA UNIVERSITY · PI FRICKER, LLOYD D · 1987 to 2015
$5.9M
Proteomics CoreP20DA026149 · NIDA · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI ANGELETTI, RUTH HOGUE · 2009 to 2011
$2.9M
FT-ICR MASS SPECTROMETER: TYPE 1 DIABETESS10RR019891 · NCRR · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI ANGELETTI, RUTH HOGUE · 2004 to 2004
$1.7M
H/D Exchange Coupled to MS to Study Drug-Induced Change in Microtuble StructureR01CA124898 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE · PI HORWITZ, SUSAN BAND · 2007 to 2010
$1.3M
MASS SPECTROMETER SYSTEM: OBESITYS10RR019352 · NCRR · ALBERT EINSTEIN COL OF MED YESHIVA UNIV · PI ANGELETTI, RUTH HOGUE · 2004 to 2004
$379k
NCI NIH HHS 1R01CA124898NCI NIH HHS R01 CA124898NCRR NIH HHS S10 RR019352NCRR NIH HHS S10 RR019891NIDA NIH HHS 1P20 DA026149NIDA NIH HHS DA-004494NIDA NIH HHS P20 DA026149NIDA NIH HHS R01 DA004494
6 · The paper itself

Abstract

The Purkinje cell degeneration (pcd) mouse has a disruption in the gene encoding cytosolic carboxypeptidase 1 (CCP1). This study tested two proposed functions of CCP1: degradation of intracellular peptides and processing of tubulin. Overexpression (2-3-fold) or knockdown (80-90%) of CCP1 in human embryonic kidney 293T cells (HEK293T) did not affect the levels of most intracellular peptides but altered the levels of α-tubulin lacking two C-terminal amino acids (delta2-tubulin) ≥ 5-fold, suggesting that tubulin processing is the primary function of CCP1, not peptide degradation. Purified CCP1 produced delta2-tubulin from purified porcine brain α-tubulin or polymerized HEK293T microtubules. In addition, CCP1 removed Glu residues from the polyglutamyl side chains of porcine brain α- and β-tubulin and also generated a form of α-tubulin with two C-terminal Glu residues removed (delta3-tubulin). Consistent with this, pcd mouse brain showed hyperglutamylation of both α- and β-tubulin. The hyperglutamylation of α- and β-tubulin and subsequent death of Purkinje cells in pcd mice was counteracted by the knock-out of the gene encoding tubulin tyrosine ligase-like-1, indicating that this enzyme hyperglutamylates α- and β-tubulin. Taken together, these results demonstrate a role for CCP1 in the processing of Glu residues from β- as well as α-tubulin in vitro and in vivo.

Indexed as

AnimalsBreast NeoplasmsCell Line, TumorColonic NeoplasmsCytosolFemaleGlutamic AcidGTP-Binding ProteinsHEK293 CellsHumansMiceMice, Inbred BALB CMice, Mutant StrainsNerve DegenerationPeptide SynthasesProtein Structure, TertiaryAgtpbp1 protein, mouseGlutamic AcidGTP-Binding ProteinsPeptide SynthasesSerine-Type D-Ala-D-Ala CarboxypeptidaseTubulintubulin polyglutamylase

Identifiers

PMID22170066
PMCPMC3307270
OpenAlexW2042089580

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.