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The CIP4 Family of F‑BAR Domain‑Containing Proteins

This chapter appears in the following book:

The Pombe Cdc15 Homology Proteins

Edited by: Pontus Aspenström
ISBN: TBA
» Get more information about this book at landesbioscience.com «

Chapter authors:
Marcia Toguchi and Pontus Aspenström


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The F‑BAR family of proteins has emerged as important coordinators of signaling pathways that regulate actomyosin assembly and membrane dynamics. This review article will focus on the Cdc42‑interacting protein 4 (CIP4) family of proteins. Recently, they have been found to bind phospholipids and participate in membrane deformation by virtue of their F‑BAR domains. These findings suggest that CIP4 family are critical linkers of membrane dynamics and actin polymerization, for instance during the internalization of transmembrane receptors. Moreover, the CIP4 family has been linked to human diseases, such as Huntington’s disease, diabetes and cancer.

Marcia Toguchi

Pontus Aspenström
Ludwig Institute for Cancer Research
Biomedical Center
Uppsala University
Uppsala, Sweden

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Additional chapters from this book:

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The CIP4 Family of F‑BAR Domain‑Containing Proteins

Marcia Toguchi and Pontus Aspenström

The F‑BAR family of proteins has emerged as important coordinators of signaling pathways that regulate actomyosin assembly and membrane dynamics. This review article will focus on the Cdc42̴...

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FES and FER: The F‑BAR Domain‑Containing Protein‑Tyrosine Kinases

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Proteins that belong to the BAR (Bin, Amphiphysin, RVS) domain superfamily are alpha‑helical bilayer‑binding modules that have evolved to induce or stabilize membrane curvature during cell...

The Budding Yeast PCH/F‑BAR Proteins

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Gas7 (growth‑arrest specific gene 7) has recently been classified to be a member of the Pombe Cdc 15 homology (PCH) family and belongs to the proline, serine, threonine‑rich phosphatase in...


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