دورية أكاديمية

Leucine retention in lysosomes is regulated by starvation.

التفاصيل البيبلوغرافية
العنوان: Leucine retention in lysosomes is regulated by starvation.
المؤلفون: Bandyopadhyay, Urmi1 bandyopu@mskcc.org, Todorova, Pavlina1, Pavlova, Natalya N.2, Tada, Yuma1, Thompson, Craig B.2,3 thompsonc@mskcc.org, Finley, Lydia W. S.1,3, Overholtzer, Michael1,3 overhom1@mskcc.org
المصدر: Proceedings of the National Academy of Sciences of the United States of America. 2/8/2022, Vol. 119 Issue 6, p1-7. 7p.
مصطلحات موضوعية: *ESSENTIAL amino acids, *LEUCINE, *LYSOSOMES, *STARVATION, *PROTEIN synthesis, *COMMERCIAL products
مستخلص: Cells acquire essential nutrients from the environment and utilize adaptive mechanisms to survive when nutrients are scarce. How nutrients are trafficked and compartmentalized within cells and whether they are stored in response to stress remain poorly understood. Here, we investigate amino acid trafficking and uncover evidence for the lysosomal transit of numerous essential amino acids. We find that starvation induces the lysosomal retention of leucine in a manner requiring RAG-GTPases and the lysosomal protein complex Ragulator, but that this process occurs independently of mechanistic target of rapamycin complex 1 activity. We further find that stored leucine is utilized in protein synthesis and that inhibition of protein synthesis releases lysosomal stores. These findings identify a regulated starvation response that involves the lysosomal storage of leucine. [ABSTRACT FROM AUTHOR]
قاعدة البيانات: Academic Search Index
الوصف
تدمد:00278424
DOI:10.1073/pnas.2114912119