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Related Experiment Videos

ACAPs are arf6 GTPase-activating proteins that function in the cell periphery.

T R Jackson1, F D Brown, Z Nie

  • 1Laboratory of Cellular Oncology, Division of Basic Sciences, National Cancer Institute, Bethesda, Maryland 20892-4255, USA.

The Journal of Cell Biology
|November 4, 2000
PubMed
Summary
This summary is machine-generated.

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Researchers identified two new Arf6 GTPase-activating proteins (GAPs), ACAP1 and ACAP2, crucial for regulating cell membrane trafficking and cytoskeleton dynamics. These GAPs specifically target Arf6, influencing membrane ruffles and protrusions.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • ADP-ribosylation factor 6 (Arf6) is a GTP-binding protein essential for endosomal trafficking and actin cytoskeleton regulation.
  • GTPase-activating proteins (GAPs) are key regulators of Arf protein function, particularly in returning Arf to its inactive GDP-bound state.

Purpose of the Study:

  • To identify and characterize novel Arf6 GAPs.
  • To investigate the role of ACAP1 and ACAP2 in Arf6-mediated cellular processes.
  • To compare the function of ACAP1 and ACAP2 with other Arf GAPs like ASAP1.

Main Methods:

  • Protein identification and characterization.
  • Expression analysis in cultured cell lines.
  • Overexpression studies in NIH 3T3 fibroblasts and HeLa cells.

Related Experiment Videos

  • In vitro substrate specificity assays.

    • Main Results:

    • ACAP1 and ACAP2 were identified as Arf6-specific GAPs.
    • Both ACAP1 and ACAP2, along with ASAP1 and PAP, belong to a protein family with conserved structural motifs and phosphoinositide-dependent GAP activity.
    • ACAP1 and ACAP2 inhibited PDGF-induced membrane ruffles and Arf6-dependent protrusions, and were recruited to peripheral tubular membranes.
    • ACAP1 and ACAP2 showed higher substrate preference for Arf6 compared to Arf1 and Arf5, unlike ASAP1.

    Conclusions:

    • ACAP1 and ACAP2 are novel Arf6 GAPs that play significant roles in regulating Arf6 activity at the cell periphery.
    • These findings highlight the distinct yet potentially coordinated functions of multiple Arf GAPs in cellular processes like membrane ruffling and protrusion formation.