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Structural mechanism of a Rag GTPase activation checkpoint by the lysosomal folliculin complex
Abstract
Cellular response to nutrient status: An intricate regulatory mechanism is taking shape around control of the mechanistic target of rapamycin complex 1 (mTORC1) protein kinase complex. Physiological responses of cells to nutrient abundance is regulated by signaling through mTORC1, which interacts with a complex of other proteins at the lysosome that includes small guanosine triphosphatases (GTPases), GTPase-activating proteins, and others. Lawrence et al. present a cryo–electron microscopy structure and biochemical experiments that reveal that the small GTPases act in unanticipated ways in the complex. The tumor suppressor folliculin (FLCN), along with FLCN-interacting protein 2, interacts with its partner GTPase RagC in both active and inactive states, suggesting that a particularly elaborate and stringent regulatory mechanism is at work. Science , this issue p. 971
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“The Folliculin (FLCN)/Folliculin-interacting protein (FNIP) complex is a critical regulator of TFEB and TFE3 activation. By promoting GDP-loading of RAGC27, FLCN facilitates interaction of TFEB/TFE3 with RAGs, resulting in retention of the transcription factors in the cytosol28,29.”
From TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress (2024) · cites this paper as [27]
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Self-citationRegulation of TORC1 by Rag GTPases in nutrient response
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Self-citationRagulator Is a GEF for the Rag GTPases that Signal Amino Acid Levels to mTORC1
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Amino acid-dependent control of mTORC1 signaling: a variety of regulatory modes
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Multi cell line analysis of lysosomal proteomes reveals unique features and novel lysosomal proteins
Akter, F., Ponnaiyan, S., Kögler-Mohrbacher, B., Bleibaum, F., Damme, M., Renard, B. Y., & Winter, D. (2020) · doi:10.1101/2020.12.21.423747 · Cited by 55
TMEM55B links autophagy flux, lysosomal repair, and TFE3 activation in response to oxidative stress
Jeong, E., Willett, R., Rissone, A., La Spina, M., & Puertollano, R. (2024) · Nature Communications · doi:10.1038/s41467-023-44316-6 · Cited by 25
Metadata
- Authors
- Lawrence, R. E., Fromm, S. A., Fu, Y., Yokom, A. L., Kim, D. J., Thelen, A. M., Young, L. N., Lim, C.-Y., Samelson, A. J., Hurley, J. H., & Zoncu, R.
- Venue
- Science
- Published
- 2019-11-22
- Volume
- 366
- Issue
- 6468
- Pages
- 971-977
- ISSN
- 0036-8075
- 1095-9203
- PMC
- PMC6945816
- Cited by
- 192
- References
- 16
- Language
- en
- Funders
- National Institutes of Health (GM111730, 1DP2CA195761-01)
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