Evidence map›Paper›PMID 7492341›Full record

ArticleThe Biochemical journal1995

The nature of topogenic sequences determines the transport competence of topological mutants of neutral endopeptidase-24.11.

X F Yang, P Crine, G Boileau

Abstract read
In one paragraph

Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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2 · The registry

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3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

3 authors.

X F YangDépartement de biochimie, Faculté de médecine, Université de Montréal, Quebec, Canada.
P Crine
G Boileau

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type II integral membrane proteins are anchored by a signal-peptide/membrane-anchor domain (SA domain) located near their N-terminus, whereas type I membrane proteins are anchored by stop-transfer sequences usually located near the C-terminus. In this study we have attempted to transform neutral endopeptidase-24.11 (EC 3.4.24.11; NEP), a type II membrane protein, into a type I membrane protein. Three type I mutant proteins were constructed by fusion of topogenic sequences to the C-terminus of SecNEP, a soluble form of NEP. The first two type I mutants, SecNEP-TMC and SecNEP-TMIC, were constructed by fusing in frame the cytosolic and SA domains of NEP to the C-terminus of SecNEP. These two fusion proteins differ only in the orientation of the cytosolic tail. The third type I mutant, SecNEP-ACE, was constructed by fusing in frame the stop-transfer and cytosolic domains of angiotensin I-converting enzyme (EC 3.4.15.1; ACE) to the C-terminus of SecNEP. Our results suggest that: (1) the NEP ectodomain can be anchored with a type I topology in the endoplasmic reticulum (ER) membrane by both NEP and ACE topogenic sequences; (2) SecNEP-TMC and SecNEP-TMIC were transport-incompetent and needed proteolytic cleavage in the C-terminal region to leave the ER, whereas SecNEP-ACE was transported out of the ER as a type I membrane protein. Therefore we concluded that the nature of topogenic sequences determines the transport-competence of topological mutants of neutral endopeptidase-24.11.

Indexed as

Amino Acid SequenceAnimalsbeta-N-AcetylhexosaminidasesBiological TransportCell LineCell MembraneEndoplasmic ReticulumGlycoside HydrolasesImmunoblottingKineticsMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedNeprilysinPeptidyl-Dipeptidase ARabbitsbeta-N-AcetylhexosaminidasesGlycoside HydrolasesMembrane ProteinsNeprilysinPeptidyl-Dipeptidase ARecombinant Fusion Proteins

Identifiers

PMID7492341
PMCPMC1136232

What OpenQuestion holds

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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.