The role of palmitoylation and transmembrane domain in sorting of transmembrane adaptor proteins
Language English Country Great Britain, England Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
26585312
DOI
10.1242/jcs.175190
PII: jcs.175190
Knihovny.cz E-resources
- Keywords
- LAT, PAG, Palmitoylation, Plasma membrane, Protein sorting, Transmembrane domain,
- MeSH
- Adaptor Proteins, Signal Transducing chemistry metabolism MeSH
- Cell Membrane metabolism MeSH
- Extracellular Space chemistry MeSH
- Glycosylation MeSH
- HEK293 Cells MeSH
- HeLa Cells MeSH
- Jurkat Cells MeSH
- Humans MeSH
- Lipoylation * MeSH
- Membrane Proteins chemistry metabolism MeSH
- Protein Structure, Tertiary MeSH
- Protein Transport MeSH
- Structure-Activity Relationship MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Adaptor Proteins, Signal Transducing MeSH
- Membrane Proteins MeSH
Plasma membrane proteins synthesised at the endoplasmic reticulum are delivered to the cell surface via sorting pathways. Hydrophobic mismatch theory based on the length of the transmembrane domain (TMD) dominates discussion about determinants required for protein sorting to the plasma membrane. Transmembrane adaptor proteins (TRAP) are involved in signalling events which take place at the plasma membrane. Members of this protein family have TMDs of varying length. We were interested in whether palmitoylation or other motifs contribute to the effective sorting of TRAP proteins. We found that palmitoylation is essential for some, but not all, TRAP proteins independent of their TMD length. We also provide evidence that palmitoylation and proximal sequences can modulate sorting of artificial proteins with TMDs of suboptimal length. Our observations point to a unique character of each TMD defined by its primary amino acid sequence and its impact on membrane protein localisation. We conclude that, in addition to the TMD length, secondary sorting determinants such as palmitoylation or flanking sequences have evolved for the localisation of membrane proteins.
References provided by Crossref.org
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