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Related Concept Videos

The Ras Gene02:38

The Ras Gene

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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.
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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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Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...
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The primary microtubule organizing center (MTOC) in animal cells is the centrosome. A centrosome has two cylindrical centrioles at its core. Each centriole consists of nine sets of three microtubules held together by proteins. The centrioles are positioned at right angles to each other and surrounded by a shapeless protein cloud called the pericentriolar matrix, or pericentriolar material (PCM).
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Microtubules are hollow cylindrical filaments having a diameter of approximately 25 nm and a length that varies from 200 nm to 25 μm. GTP-bound tubulin subunits form αβ-heterodimers for microtubule assembly. These core building blocks interact longitudinally, polymerizing into protofilaments. The protofilaments then interact with one another through lateral bonding forces to form stable cylindrical microtubules. These cylindrical filaments are dynamic as they undergo repeated...
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Quantitative Immunofluorescence Assay to Measure the Variation in Protein Levels at Centrosomes
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Truncated RASSF7 promotes centrosomal defects and cell death.

Tulay Gulsen1, Irene Hadjicosti1, Yueshi Li1

  • 1Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, United Kingdom.

Developmental Biology
|November 17, 2015
PubMed
Summary

The coiled-coil domain of RASSF7 protein directs its centrosome localization. Truncated RASSF7 causes centrosome defects and cell death, suggesting a potential oncogenic role in some cancers.

Keywords:
Cell deathCentrosomeMitosisOncogeneRASSF7Xenopus

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Area of Science:

  • Cell Biology
  • Molecular Oncology

Background:

  • RASSF7 protein localizes to the centrosome and is implicated in mitosis.
  • Elevated RASSF7 expression is observed in various tumor types, but its oncogenic potential and molecular functions remain unclear.

Purpose of the Study:

  • To investigate the molecular basis of RASSF7's centrosomal localization.
  • To determine the role of specific RASSF7 domains in its localization and function.
  • To explore the potential oncogenic activity of RASSF7, particularly in its truncated forms.

Main Methods:

  • Generation and expression of truncated RASSF7 constructs in Xenopus embryos.
  • Quantification of centrosomal localization for each RASSF7 variant.
  • Analysis of centrosome defects, including γ-tubulin accumulation and amplification.
  • Bioinformatic analysis of tumor databases for RASSF7 mutations.

Main Results:

  • The coiled-coil domain of RASSF7 is both necessary and sufficient for centrosomal localization.
  • The RA domain does not play a significant role in RASSF7 localization.
  • Truncation of the C-terminus leads to RASSF7 accumulation at the centrosome, causing defects like γ-tubulin accumulation and amplification.
  • Cells expressing C-terminally truncated RASSF7 exhibit increased cell death.
  • A tumor database analysis revealed a mutation causing a similar C-terminal truncation.

Conclusions:

  • RASSF7's coiled-coil domain is critical for its centrosome targeting.
  • C-terminal truncation of RASSF7 induces centrosome abnormalities and cell death, mediated by its coiled-coil domain.
  • Truncated RASSF7 represents a potential oncogenic driver in a subset of tumors with specific mutations.