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Related Concept Videos

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Rab Cascades

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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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Rab Proteins01:14

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Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
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Protein Complex Assembly02:41

Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Assembly of Signaling Complexes01:30

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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Protein Translocation Machinery on the ER Membrane01:28

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Related Experiment Video

Updated: Nov 21, 2025

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Structural insights into TSC complex assembly and GAP activity on Rheb.

Huirong Yang1,2,3,4, Zishuo Yu5, Xizi Chen5

  • 1Fudan University Shanghai Cancer Center, Institutes of Biomedical Sciences, State Key Laboratory of Genetic Engineering and Shanghai Key Laboratory of Medical Epigenetics, Shanghai Medical College of Fudan University, Shanghai, 200032, China. yanghr@fudan.edu.cn.

Nature Communications
|January 13, 2021
PubMed
Summary
This summary is machine-generated.

The study reveals the near-atomic structure of the Tuberous Sclerosis Complex (TSC), detailing its arch-shaped architecture and how it regulates cell growth by inhibiting mTORC1. This provides insights into TSC assembly and its GTPase-activating protein function.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Tuberous Sclerosis Complex (TSC) regulates cell growth by controlling mTORC1 activity.
  • TSC functions as a GTPase-activating protein (GAP) for Rheb, inhibiting mTORC1 activation.
  • Mutations in TSC genes are linked to tuberous sclerosis.

Purpose of the Study:

  • To determine the near-atomic resolution structure of the human TSC complex.
  • To elucidate the mechanisms of TSC complex assembly.
  • To understand the structural basis of TSC's GTPase-activating protein (GAP) activity.

Main Methods:

  • Near-atomic resolution cryo-electron microscopy
  • X-ray crystallography
  • Biochemical assays

Main Results:

  • Revealed an arch-shaped architecture of the human TSC complex with a 2:2:1 stoichiometry of TSC1, TSC2, and TBC1D7.
  • Described the asymmetric assembly involving interweaved TSC1 coiled-coils, TBC1D7, and a tail-to-tail TSC2 dimer.
  • Identified complementary interactions between TSC2 GAP domains and Rheb, proposing a catalytic mechanism involving an asparagine thumb (N1643) for GTP hydrolysis.

Conclusions:

  • The study provides a structural framework for understanding TSC complex assembly and its regulation of Rheb.
  • Insights into the catalytic mechanism of TSC's GAP activity offer potential targets for therapeutic interventions.
  • The findings deepen our understanding of the molecular basis of tuberous sclerosis.