| First Author | Jin Q | Year | 2012 |
| Journal | Biochem Biophys Res Commun | Volume | 428 |
| Issue | 3 | Pages | 333-8 |
| PubMed ID | 23079622 | Mgi Jnum | J:190689 |
| Mgi Id | MGI:5449473 | Doi | 10.1016/j.bbrc.2012.10.047 |
| Citation | Jin Q, et al. (2012) Role of km23-1 in RhoA/actin-based cell migration. Biochem Biophys Res Commun 428(3):333-8 |
| abstractText | km23-1 was originally identified as a TGFss receptor-interacting protein that plays an important role in TGFss signaling. Moreover, km23-1 is actually part of an ancient superfamily of NTPase-regulatory proteins, widely represented in archaea and bacteria. To further elucidate the function of km23-1, we identified novel protein interacting partners for km23-1 by using tandem affinity purification (TAP) and tandem mass spectrometry (MS). Here we show that km23-1 interacted with a class of proteins involved in actin-based cell motility and modulation of the actin cytoskeleton. We further showed that km23-1 modulates the formation of a highly organized stress fiber network. More significantly, we demonstrated that knockdown (KD) of km23-1 decreased RhoA activation in Mv1Lu epithelial cells. Finally, our results demonstrated for the first time that depletion of km23-1 inhibited cell migration of human colon carcinoma cells (HCCCs) in wound-healing assays. Overall, our findings demonstrate that km23-1 regulates RhoA and motility-associated actin modulating proteins, suggesting that km23-1 may represent a novel target for anti-metastatic therapy. |
