Unknown

Dataset Information

0

Tks adaptor proteins at a glance.


ABSTRACT: Tyrosine kinase substrate (Tks) adaptor proteins are considered important regulators of various physiological and/or pathological processes, particularly cell migration and invasion, and cancer progression. These proteins contain PX and SH3 domains, and act as scaffolds, bringing membrane and cellular components in close proximity in structures known as invadopodia or podosomes. Tks proteins, analogous to the related proteins p47phox, p40phox and NoxO1, also facilitate local generation of reactive oxygen species (ROS), which aid in signaling at invadopodia and/or podosomes to promote their activity. As their name suggests, Tks adaptor proteins are substrates for tyrosine kinases, especially Src. In this Cell Science at a Glance article and accompanying poster, we discuss the known structural and functional aspects of Tks adaptor proteins. As the science of Tks proteins is evolving, this article will point out where we stand and what still needs to be explored. We also underscore pathological conditions involving these proteins, providing a basis for future research to develop therapies for treatment of these diseases.

SUBMITTER: Saini P 

PROVIDER: S-EPMC5818055 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature

altmetric image

Publications

Tks adaptor proteins at a glance.

Saini Priyanka P   Courtneidge Sara A SA  

Journal of cell science 20180108 1


Tyrosine kinase substrate (Tks) adaptor proteins are considered important regulators of various physiological and/or pathological processes, particularly cell migration and invasion, and cancer progression. These proteins contain PX and SH3 domains, and act as scaffolds, bringing membrane and cellular components in close proximity in structures known as invadopodia or podosomes. Tks proteins, analogous to the related proteins p47<sup>phox</sup>, p40<sup>phox</sup> and NoxO1, also facilitate loca  ...[more]

Similar Datasets

| S-EPMC3425387 | biostudies-literature
| S-EPMC5346654 | biostudies-literature
| S-EPMC4117225 | biostudies-literature
| S-EPMC3924200 | biostudies-literature
| S-EPMC5902548 | biostudies-literature
| PRJNA195946 | ENA
| S-EPMC3013238 | biostudies-literature
| S-EPMC5192565 | biostudies-literature
| S-EPMC3832257 | biostudies-literature
| S-EPMC8187788 | biostudies-literature