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Electroporation of Functional Bacterial Effectors into Mammalian Cells
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CRIB effector disorder: exquisite function from chaos.

Darerca Owen1, Helen R Mott2

  • 1Department of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, U.K. do202@cam.ac.uk.

Biochemical Society Transactions
|August 30, 2018
PubMed
Summary
This summary is machine-generated.

Cdc42/Rac interactive binding (CRIB) proteins utilize intrinsically disordered regions and basic regions to bind G-proteins. This interaction drives liquid-liquid phase separation, crucial for forming cellular signalosomes.

Keywords:
CRIB effectorsintrinsically disordered proteinsprotein conformationsmall G-proteins

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Area of Science:

  • Molecular and Cellular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Cdc42/Rac interactive binding (CRIB) proteins are effectors of small G-proteins.
  • These proteins feature intrinsically disordered regions (IDRs) and basic regions (BRs).

Purpose of the Study:

  • To elucidate the structural and functional roles of IDRs and BRs in CRIB proteins.
  • To understand how these regions mediate G-protein binding and signalosome formation.

Main Methods:

  • Analysis of protein structure and disorder.
  • Investigation of protein-protein interactions.
  • Studies on liquid-liquid phase separation.

Main Results:

  • G-protein binding regions within CRIB proteins are intrinsically disordered.
  • Basic regions in CRIB proteins facilitate G-protein binding via a dock-and-coalesce mechanism.
  • Intrinsically disordered regions and basic regions enable multivalent interactions, driving liquid-liquid phase separation and signalosome assembly.

Conclusions:

  • The structural plasticity of CRIB proteins, particularly their IDRs and BRs, is essential for their function.
  • These features allow CRIB proteins to mediate G-protein interactions and initiate signalosome formation through liquid-liquid phase separation.