A novel c‐Src recruitment pathway from the cytosol to focal adhesions

Abstract

The role of myristoylation in the localization and catalytic activity of Src at focal adhesions was investigated by live-cell imaging and site-directed mutagenesis. Although the majority of activated Src molecules are localized at focal adhesions, it is unclear how activated Src molecules are recruited to focal adhesions. Because Src is activated at the cell membrane, translocation of Src to cell membranes is considered to be essential for its recruitment to focal adhesions. Membrane-targeting-deficient Src mutant SrcG2A localizes at focal adhesions, indicating direct recruitment of Src from cytosol to focal adhesions. Furthermore, directly recruited Src molecules are shown to enhance paxillin dynamics at focal adhesions. These results reveal that the regulation of Src activation and translocation is more complex than previously suggested.

Cabazitaxel-loaded poly(alkyl cyanoacrylate) nanoparticles: Toxicity and changes in the proteome of breast, colon and prostate cancer cells

“…CSK is a non-receptor tyrosine-protein kinase that regulates cell growth, differentiation, migration and immune response, and phosphorylates tyrosine residues located in the C-terminal tails not only of SRC, but also of other SRC-family kinases such as LCK, HCK, FYN, LYN, CSK or YES1 (Indovina et al 2017). CSK has been shown to suppress signaling by various surface receptors, including T-and B-cell receptors by phosphorylating and maintaining inactive several positive effectors such as FYN, SRC or LCK (Horejsi 2004;Machiyama et al 2017).…”

ARHGAP4-SEPT2-SEPT9 complex enables both up- and down-modulation of integrin-mediated focal adhesions, cell migration, and invasion

“…Focal adhesions (FAs) are sites that connect extracellular matrix (ECM) proteins and intracellular actin bundles to regulate multiple cellular processes such as migration and invasion (Carragher & Frame, 2004;Machiyama, Yamaguchi, Watanabe, & Fujita, 2017;Paluch, Aspalter, & Sixt, 2016;Wozniak, Modzelewska, Kwong, & Keely, 2004). Among the proteins that constitute FAs, integrin serves as a transmembrane receptor that exists in a heterodimer composed of different types of α and β subunits.…”