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Related Experiment Videos

Ras (CXXX) and Rab (CC/CXC) prenylation signal sequences are unique and functionally distinct.

R Khosravi-Far1, G J Clark, K Abe

  • 1Department of Pharmacology, Lineberger Cancer Center, University of North Carolina, Chapel Hill 27599.

The Journal of Biological Chemistry
|December 5, 1992
PubMed
Summary
This summary is machine-generated.

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Rab proteins require complex sequences, not just CC/CXC motifs, for isoprenoid modification. A shared geranylgeranyl transferase modifies Rab proteins, suggesting conformational recognition is key.

Area of Science:

  • Molecular Biology
  • Protein Modification
  • Cellular Signaling

Background:

  • Rab proteins are crucial for intracellular transport.
  • Isoprenoid modification is essential for the function of many proteins, including Ras.
  • Rab proteins utilize CC or CXC terminal motifs, unlike the CXXX motif in Ras.

Purpose of the Study:

  • To investigate the sequence requirements for Rab protein isoprenoid modification.
  • To compare the functional relationship between Ras CXXX and Rab CC/CXC motifs.
  • To determine if Rab CC/CXC motifs can substitute for the Ras CXXX motif in signaling isoprenoid modification.

Main Methods:

  • Generation of chimeric Ras proteins with Rab carboxyl-terminal sequences.
  • In vitro and in vivo isoprenylation assays.

Related Experiment Videos

  • Competition studies using geranylgeranyl transferase.

    • Main Results:

    • Chimeric Ras proteins with Rab CC/CXC motifs were not isoprenylated.
    • Extended Rab carboxyl-terminal sequences in chimeric proteins also failed to induce isoprenylation.
    • Competition assays confirmed a common geranylgeranyl transferase activity for Rab proteins.

    Conclusions:

    • Rab protein isoprenoid modification is more complex than the Ras CXXX motif.
    • Rab geranylgeranyl transferase likely recognizes protein conformation for modification.
    • A single geranylgeranyl transferase activity modifies Rab proteins with CC or CXC motifs.