The role of prolines and glycine in the transmembrane domain of LAT
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388955%3A_____%2F21%3A00539844" target="_blank" >RIV/61388955:_____/21:00539844 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/21:00554617 RIV/00216208:11310/21:10440413
Result on the web
<a href="https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15713" target="_blank" >https://febs.onlinelibrary.wiley.com/doi/full/10.1111/febs.15713</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/febs.15713" target="_blank" >10.1111/febs.15713</a>
Alternative languages
Result language
angličtina
Original language name
The role of prolines and glycine in the transmembrane domain of LAT
Original language description
Linker for activation in T cells (LAT) is a critical regulator of T‐cell development and function. It organises signalling events at the plasma membrane. However, the mechanism, which controls LAT localisation at the plasma membrane, is not fully understood. Here, we studied the impact of helix‐breaking amino acids, two prolines and one glycine, in the transmembrane segment on localisation and function of LAT. Using in silico analysis, confocal and super‐resolution imaging and flow cytometry, we demonstrate that central proline residue destabilises transmembrane helix by inducing a kink. The helical structure and dynamics are further regulated by glycine and another proline residue in the luminal part of LAT transmembrane domain. Replacement of these residues with aliphatic amino acids reduces LAT dependence on palmitoylation for sorting to the plasma membrane. However, surface expression of these mutants is not sufficient to recover function of nonpalmitoylated LAT in stimulated T cells. These data indicate that geometry and dynamics of LAT transmembrane segment regulate its localisation and function in immune cells.n
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
FEBS Journal
ISSN
1742-464X
e-ISSN
1742-4658
Volume of the periodical
288
Issue of the periodical within the volume
13
Country of publishing house
US - UNITED STATES
Number of pages
14
Pages from-to
4039-4052
UT code for WoS article
000617213100001
EID of the result in the Scopus database
2-s2.0-85100974966