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Related Concept Videos

Yeast Signaling01:28

Yeast Signaling

Yeasts are single-celled organisms, but unlike bacteria, they are eukaryotes (cells with a nucleus). Cell signaling in yeast is similar to signaling in other eukaryotic cells. A ligand, such as a protein or a small molecule released from a yeast cell, attaches to a receptor on the cell surface. The binding stimulates second-messenger kinases to activate or inactivate transcription factors that further regulate gene expression. Many of the yeast intracellular signaling cascades have similar...
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Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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The Ras Gene02:38

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...
Small GTPases - Ras and Rho01:24

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
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MAPK Signaling Cascades01:07

MAPK Signaling Cascades

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Assay for Adhesion and Agar Invasion in S. cerevisiae
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Published on: November 8, 2006

The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast.

K Scheffzek1, P Grünewald, S Wohlgemuth

  • 1Max-Planck-Institut für molekulare Physiologie, Abt. Strukturelle Biologie, Otto-Hahn-Str. 11, 44227, Dortmund, Germany.

Structure (London, England : 1993)
|November 16, 2001
PubMed
Summary

Researchers elucidated the Ras-Byr2 complex structure, revealing conserved Ras-effector interactions in yeast. An additional helical segment in Byr2 may play a role in kinase activation, offering insights into cancer-related signaling pathways.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Ras GTPase is crucial for cell growth and differentiation, with mutations driving cancer by maintaining constitutive activity.
  • Ras proteins activate downstream signaling cascades, often involving kinase pathways, but the precise activation mechanism remains unclear.
  • Understanding Ras-effector interactions is vital, yet structural data for non-mammalian systems are limited.

Purpose of the Study:

  • To determine the structural basis of Ras-effector interactions using the Schizosaccharomyces pombe Byr2 kinase as a model.
  • To investigate the conserved mechanisms of Ras signaling in a lower eukaryotic system.
  • To identify novel structural features that may contribute to kinase activation.

Main Methods:

  • X-ray crystallography was employed to determine the structure of the Ras-Byr2 Ras binding domain (RBD) complex.
  • The complex was analyzed at 3 Å resolution to elucidate interprotein interactions and structural architecture.
  • Bioinformatic and structural comparisons were made with known mammalian Ras-effector complexes.

Main Results:

  • The crystal structure revealed a conserved complex architecture between Ras and Byr2RBD, featuring an interprotein beta sheet stabilized by polar interactions.
  • Key contact points were identified within the Ras switch I region and across topologically distinct regions of Byr2.
  • A novel C-terminal helical segment in Byr2, absent in mammalian homologs, was found to possess an additional binding site outside the switch I region.

Conclusions:

  • The Ras-Byr2 complex structure validates the Ras binding module as a conserved communication element mediating Ras-effector interactions.
  • The conservation of Ras-effector complex architecture in yeast highlights a fundamental signaling mechanism across eukaryotes.
  • The identified C-terminal helical segment in Byr2 is proposed to play a role in kinase activation, potentially representing a novel regulatory mechanism.