Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways. Issue 4 (21st June 2021)
- Record Type:
- Journal Article
- Title:
- Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways. Issue 4 (21st June 2021)
- Main Title:
- Looking for a safe haven: tail-anchored proteins and their membrane insertion pathways
- Authors:
- Mehlhorn, Dietmar G
Asseck, Lisa Y
Grefen, Christopher - Abstract:
- Abstract: Insertion of membrane proteins into the lipid bilayer is a crucial step during their biosynthesis. Eukaryotic cells face many challenges in directing these proteins to their predestined target membrane. The hydrophobic signal peptide or transmembrane domain (TMD) of the nascent protein must be shielded from the aqueous cytosol and its target membrane identified followed by transport and insertion. Components that evolved to deal with each of these challenging steps range from chaperones to receptors, insertases, and sophisticated translocation complexes. One prominent translocation pathway for most proteins is the signal recognition particle (SRP)-dependent pathway which mediates co-translational translocation of proteins across or into the endoplasmic reticulum (ER) membrane. This textbook example of protein insertion is stretched to its limits when faced with secretory or membrane proteins that lack an amino-terminal signal sequence or TMD. Particularly, a large group of so-called tail-anchored (TA) proteins that harbor a single carboxy-terminal TMD require an alternative, post-translational insertion route into the ER membrane. In this review, we summarize the current research in TA protein insertion with a special focus on plants, address challenges, and highlight future research avenues. Abstract : Update on different pathways and candidates that facilitate membrane insertion of tail-anchored proteins in eukaryotes with a special emphasis on recent insights inAbstract: Insertion of membrane proteins into the lipid bilayer is a crucial step during their biosynthesis. Eukaryotic cells face many challenges in directing these proteins to their predestined target membrane. The hydrophobic signal peptide or transmembrane domain (TMD) of the nascent protein must be shielded from the aqueous cytosol and its target membrane identified followed by transport and insertion. Components that evolved to deal with each of these challenging steps range from chaperones to receptors, insertases, and sophisticated translocation complexes. One prominent translocation pathway for most proteins is the signal recognition particle (SRP)-dependent pathway which mediates co-translational translocation of proteins across or into the endoplasmic reticulum (ER) membrane. This textbook example of protein insertion is stretched to its limits when faced with secretory or membrane proteins that lack an amino-terminal signal sequence or TMD. Particularly, a large group of so-called tail-anchored (TA) proteins that harbor a single carboxy-terminal TMD require an alternative, post-translational insertion route into the ER membrane. In this review, we summarize the current research in TA protein insertion with a special focus on plants, address challenges, and highlight future research avenues. Abstract : Update on different pathways and candidates that facilitate membrane insertion of tail-anchored proteins in eukaryotes with a special emphasis on recent insights in plant research. … (more)
- Is Part Of:
- Plant physiology. Volume 187:Issue 4(2021)
- Journal:
- Plant physiology
- Issue:
- Volume 187:Issue 4(2021)
- Issue Display:
- Volume 187, Issue 4 (2021)
- Year:
- 2021
- Volume:
- 187
- Issue:
- 4
- Issue Sort Value:
- 2021-0187-0004-0000
- Page Start:
- 1916
- Page End:
- 1928
- Publication Date:
- 2021-06-21
- Subjects:
- Plant physiology -- Periodicals
Botany -- Periodicals
Periodicals
Electronic journals
571.2 - Journal URLs:
- https://academic.oup.com/plphys/issue ↗
http://www.plantphysiol.org/ ↗
http://www.jstor.org/journals/00320889.html ↗
http://www.pubmedcentral.nih.gov/tocrender.fcgi?journal=69 ↗
http://www-us.ebsco.com/online/direct.asp?JournalID=101725 ↗
http://www.oxfordjournals.org/ ↗ - DOI:
- 10.1093/plphys/kiab298 ↗
- Languages:
- English
- ISSNs:
- 0032-0889
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 25008.xml