The WASp homologue Las17p functions with the WIP homologue End5p/verprolin and is essential for endocytosis in yeast
- 27 August 1998
- journal article
- research article
- Published by Elsevier
- Vol. 8 (17) , S1-S3
- https://doi.org/10.1016/s0960-9822(98)70396-3
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Actin-binding Verprolin Is a Polarity Development Protein Required for the Morphogenesis and Function of the Yeast Actin CytoskeletonThe Journal of cell biology, 1997
- WIP, a protein associated with Wiskott–Aldrich syndrome protein, induces actin polymerization and redistribution in lymphoid cellsProceedings of the National Academy of Sciences, 1997
- Bee1, a Yeast Protein with Homology to Wiscott-Aldrich Syndrome Protein, Is Critical for the Assembly of Cortical Actin CytoskeletonThe Journal of cell biology, 1997
- Actin-, myosin- and ubiquitin-dependent endocytosisCellular and Molecular Life Sciences, 1996
- Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase Cdc42.Proceedings of the National Academy of Sciences, 1996
- Wiskott–Aldrich Syndrome Protein, a Novel Effector for the GTPase CDC42Hs, Is Implicated in Actin PolymerizationCell, 1996
- Two GTPases, Cdc42 and Rac, bind directly to a protein implicated in the immunodeficiency disorder Wiskott–Aldrich syndromeCurrent Biology, 1996
- end5, end6, and end7: mutations that cause actin delocalization and block the internalization step of endocytosis in Saccharomyces cerevisiae.Molecular Biology of the Cell, 1995
- A proline‐rich protein, verprolin, involved in cytoskeletal organization and cellular growth in the yeast Saccharomyces cerevisiaeMolecular Microbiology, 1993
- end3 and end4: two mutants defective in receptor-mediated and fluid-phase endocytosis in Saccharomyces cerevisiae.The Journal of cell biology, 1993