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Endosidin2 targets conserved exocyst complex subunit EXO70 to inhibit exocytosis
C. Zhang, MQ. Brown, W. van de Ven, ZM. Zhang, B. Wu, MC. Young, L. Synek, D. Borchardt, R. Harrison, S. Pan, N. Luo, YM. Huang, YJ. Ghang, N. Ung, R. Li, J. Isley, D. Morikis, J. Song, W. Guo, RJ. Hooley, CE. Chang, Z. Yang, V. Zarsky, GK....
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, Non-P.H.S.
NLK
Free Medical Journals
od 1915 do Před 6 měsíci
Freely Accessible Science Journals
od 1915 do Před 6 měsíci
PubMed Central
od 1915 do Před 6 měsíci
Europe PubMed Central
od 1915 do Před 6 měsíci
Open Access Digital Library
od 1915-01-01
Open Access Digital Library
od 1915-01-15
PubMed
26607451
DOI
10.1073/pnas.1521248112
Knihovny.cz E-zdroje
- MeSH
- Arabidopsis metabolismus MeSH
- buněčná membrána metabolismus MeSH
- endozomy metabolismus MeSH
- exocytóza * MeSH
- konzervovaná sekvence MeSH
- lidé MeSH
- limoniny metabolismus MeSH
- molekulární evoluce MeSH
- proteiny huseníčku chemie genetika metabolismus MeSH
- sekundární struktura proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
The exocyst complex regulates the last steps of exocytosis, which is essential to organisms across kingdoms. In humans, its dysfunction is correlated with several significant diseases, such as diabetes and cancer progression. Investigation of the dynamic regulation of the evolutionarily conserved exocyst-related processes using mutants in genetically tractable organisms such as Arabidopsis thaliana is limited by the lethality or the severity of phenotypes. We discovered that the small molecule Endosidin2 (ES2) binds to the EXO70 (exocyst component of 70 kDa) subunit of the exocyst complex, resulting in inhibition of exocytosis and endosomal recycling in both plant and human cells and enhancement of plant vacuolar trafficking. An EXO70 protein with a C-terminal truncation results in dominant ES2 resistance, uncovering possible distinct regulatory roles for the N terminus of the protein. This study not only provides a valuable tool in studying exocytosis regulation but also offers a potentially new target for drugs aimed at addressing human disease.
Center for Molecular Communication and Signaling Wake Forest University Winston Salem NC 27109
Department of Biochemistry University of California Riverside CA 92521
Department of Bioengineering University of California Riverside CA 92521
Department of Biology University of Pennsylvania Philadelphia PA 19104
Department of Biology Wake Forest University Winston Salem NC 27109
Department of Botany and Plant Sciences University of California Riverside CA 92521
Department of Chemistry University of California Riverside CA 92521
Institute of Experimental Botany Academy of Sciences 165 02 Prague 6 Czech Republic
Citace poskytuje Crossref.org
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