Interaction of POB1, a Downstream Molecule of Small G Protein Ral, with PAG2, a Paxillin-binding Protein, Is Involved in Cell Migration

Paxillin: Adapting to Change

“…Paxillin can also interact with talin (223), poly(A)-binding protein 1 (307), ASAP1/2 (128,195), the nerve growth factor (NGF) receptor TrkA (178), the antiapoptosis protein bcl-2 (254,255), the focal adhesion protein TES (69), RACK (42), the serine/threonine phosphatase PP2A (110), the tyrosine phosphatase PTP- (206), Crk and CrkL (19,225,232), the tyrosine kinases Abl (143) and p210BCR/ABL (225), the protooncogene Cbl (224), and LIM kinase (62). Paxillin and Hic-5 also bind to the syndecan binding protein syndesmos (52), Hsp27 (118), Hsp72 (172), and the ring-finger ubiquitination component Rnf5 (54).…”

REPS2 (RALBP1 associated Eps domain containing 2)

“…The ability to suppress fibronectindependent migration depends on the ArfGAP domain of PAG2, but not on the POB1-binding domain, of PAG2. On the other end, POB1, but not POB1(PA), can suppress the inhibitory action of PAG2 on paxillin localization to focal adhesion (Oshiro et al, 2002). These results suggest that POB1, by binding to PAG2, suppresses the inhibitory action of PAG2 on the paxillin recruitment to focal contacts.…”

Expression and Clinical Significance of REPS2 in Human Esophageal Squamous Cell Carcinoma

“…Overexpression of Rac1 and Cdc42 have been reported in several types of human cancer including esophageal cancer (Bashir et al, 2010;Feng et al, 2012). Moreover, the latest published report indicated that REPS2 inhibited cell migration by interaction with the paxillin-associated protein PAG2 through its proline-rich motif (Oshiro et al, 2002). It is widely accepted that cell migration is critical for tumour formation and metastasis.…”

“…Likewise, augmentation of cellular levels of REPS2 and Hsf-1 result in dramatic apoptosis in non-small cell lung cancer cell line H358 through RalBP1 inhibition (Singhal et al, 2008). What is more, the binding of REPS2 to PAG2 inhibits cell migration (Oshiro et al, 2002). At present, REPS2 isoform 2 downregulation has been demonstrated in the progression of prostate cancer and the overexpression of REPS2 might serve as a useful biomarker for favorable prognosis in prostate and breast cancers (Oosterhoff et al, 2003;Oosterhoff et al, 2005;Doolan et al, 2009).…”

“…This gene is located on the human X chromosome at Xp22 and it has an EH domain in its N-terminal region and two proline-rich motifs and a coiled-coil structure in its C-terminal region. The two proline-rich regions of REPS2 have been shown to interact with the growth factor receptor adaptor protein Grb2 (Ikeda et al, 1998) and the paxillin-associated protein PAG2 (Oshiro et al, 2002), while the EH domain of REPS2 is found to bind directly to Epsin and Eps15 (Chen et al, 1998;Morinaka et al, 1999;Kariya et al, 2000).…”