Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton.

@article{Salazar2003TubaAN,
  title={Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton.},
  author={Marco Antonio Oliver Salazar and Adam V Kwiatkowski and Lorenzo Pellegrini and Gianluca Cestra and Margaret H. Butler and Kent L. Rossman and Daniel M Serna and John E Sondek and Frank B. Gertler and Pietro De Camilli},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 49},
  pages={49031-43}
}
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… CONTINUE READING