ArticleThe Biochemical journal1994
Targeting of passenger protein domains to multiple intracellular membranes.
Article in The Biochemical journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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.
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Who cites it
7 citing papers in PubMed.
- The approaches for manipulating mitochondrial proteome.Environmental and molecular mutagenesis · 2010Review
- Structural insights into tail-anchored protein binding and membrane insertion by Get3.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Distinct targeting pathways for the membrane insertion of tail-anchored (TA) proteins.Journal of cell science · 2008Article
- The C-terminus of cytochrome b5 confers endoplasmic reticulum specificity by preventing spontaneous insertion into membranes.The Biochemical journal · 2007Article
- Novel targeting signals mediate the sorting of different isoforms of the tail-anchored membrane protein cytochrome b5 to either endoplasmic reticulum or mitochondria.The Plant cell · 2004Article
- Bcl-2 mutants with restricted subcellular location reveal spatially distinct pathways for apoptosis in different cell types.The EMBO journal · 1996Article
- The signal recognition particle receptor alpha subunit assembles co-translationally on the endoplasmic reticulum membrane during an mRNA-encoded translation pause in vitro.The EMBO journal · 1996Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The role of passenger domains in protein targeting was examined by fusing previously characterized targeting motifs to different protein sequences. To compare the targeting requirements for a variety of subcellular compartments, targeting of the fusion proteins was examined for endoplasmic reticulum, mitochondria and peroxisomes in vitro and in yeast. Although most passenger domains were only partially passive to translocation, motif-dependent targeting via motifs positioned at either end of one passenger domain (gPA) was demonstrated for all of the subcellular compartments tested. The data presented extend earlier suggestions that translocation competence is an intrinsic property of the passenger protein. However, the properties that determine protein targeting are not mutually exclusive for the compartments tested. Therefore, although the primary determinant of specificity is the targeting motif, our results suggest that translocation competence of the targeted protein augments the fidelity of transport.
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Registered trials
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