Tuba, a Novel Protein Containing Bin/Amphiphysin/Rvs and Dbl Homology Domains, Links Dynamin to Regulation of the Actin Cytoskeleton

Tuba is a novel scaffold protein that functions to bring together dynamin with actin regulatory proteins. It is concentrated at synapses in brain and binds dynamin selectively through four N-terminal Src homology-3 (SH3) domains. Tuba binds a variety of actin regulatory proteins, including N-WASP, C...

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Bibliographic Details
Published in:The Journal of biological chemistry 2003-12, Vol.278 (49), p.49031-49043
Main Authors: Salazar, Marco A., Kwiatkowski, Adam V., Pellegrini, Lorenzo, Cestra, Gianluca, Butler, Margaret H., Rossman, Kent L., Serna, Daniel M., Sondek, John, Gertler, Frank B., De Camilli, Pietro
Format: Article
Language:English
Subjects:
Actins - metabolism
Amino Acid Sequence
Animals
Brain - metabolism
Cytoskeletal Proteins - chemistry
Cytoskeletal Proteins - metabolism
Cytoskeleton - metabolism
Dynamins - metabolism
Immunohistochemistry
Mitochondria - metabolism
Molecular Sequence Data
Nerve Tissue Proteins - metabolism
Rats
Retroviridae Proteins, Oncogenic - metabolism
Sequence Homology, Amino Acid
Two-Hybrid System Techniques
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Summary:Tuba is a novel scaffold protein that functions to bring together dynamin with actin regulatory proteins. It is concentrated at synapses in brain and binds dynamin selectively through four N-terminal Src homology-3 (SH3) domains. Tuba binds a variety of actin regulatory proteins, including N-WASP, CR16, WAVE1, WIRE, PIR121, NAP1, and Ena/VASP proteins, via a C-terminal SH3 domain. Direct binding partners include N-WASP and Ena/VASP proteins. Forced targeting of the C-terminal SH3 domain to the mitochondrial surface can promote accumulation of F-actin around mitochondria. A Dbl homology domain present in the middle of Tuba upstream of a Bin/amphiphysin/Rvs (BAR) domain activates Cdc42, but not Rac and Rho, and may thus cooperate with the C terminus of the protein in regulating actin assembly. The BAR domain, a lipid-binding module, may functionally replace the pleckstrin homology domain that typically follows a Dbl homology domain. The properties of Tuba provide new evidence for a close functional link between dynamin, Rho GTPase signaling, and the actin cytoskeleton.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M308104200