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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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Structural basis for semaphorin signalling through the plexin receptor.

Terukazu Nogi1, Norihisa Yasui, Emiko Mihara

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Semaphorin-plexin signaling involves a structural switch from homodimers to heterotetramers, revealing how cell surface receptor activation transmits signals to the cell interior.

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Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Structural Biology

Background:

  • Semaphorins and plexins are crucial cell-signaling molecules involved in various biological processes and human diseases.
  • Ligand binding to plexin receptors activates intracellular GTPase-activating protein (GAP) activity, but the structural mechanism is unclear.

Purpose of the Study:

  • To elucidate the structural mechanism of semaphorin-plexin receptor activation.
  • To determine the structures of semaphorin 6A (Sema6A) and plexin A2 (PlxnA2) in pre- and post-binding states.

Main Methods:

  • X-ray crystallography was used to determine the structures of Sema6A and PlxnA2 fragments.
  • Complex structures of Sema6A-PlxnA2 were analyzed.
  • Cell-based activity assays with mutant ligands/receptors were performed.

Main Results:

  • Sema6A formed a 'face-to-face' homodimer, while PlxnA2 adopted an 'head-on' homodimer arrangement before binding.
  • The Sema6A-PlxnA2 complex formed a 2:2 heterotetramer, with PlxnA2 undergoing 'partner exchange' by dissociating and docking onto the Sema6A homodimer.
  • The 'face-to-face' homodimer arrangement of Sema6A is physiologically relevant and maintained during signaling.

Conclusions:

  • Plexin homodimer-to-heterodimer transitions are key to signal transmission.
  • These transitions reorient the plexin's molecular axis, facilitating signal transfer to the cytoplasmic region and inducing GAP domain activation.