Example sentences for: yqxp

How can you use “yqxp” in a sentence? Here are some example sentences to help you improve your vocabulary:

  • The adaptor protein Cas has several domains that are important for its function, an SH3 domain, a central substrate domain with up to 15 tyrosines that can serve as tyrosine kinase substrates for upstream kinases such as Src and Abl [ 19 42 43 ] , and a C-terminal Src binding domain with PXXP motifs for binding to the SH3 domain of Src, and two tyrosines providing docking sites for the Src SH2 domain upon phosphorylation [ 6 ] . The substrate domain of Cas has two major types of tyrosine motifs that can be phosphorylated and bind downstream effectors, YQXP (4 copies) and YDXP motifs (9 copies), suggesting that at least two classes of downstream effectors, one capable of binding to YDXP motifs and the other capable of binding to YQXP motifs, are assembled by this adaptor protein.

  • These data indicate that the v-crk SH2 domain interacts with the C-terminal YDXP motifs, and as suggested by Birge et al, v-crk may be able to protect them from dephosphorylation and/or induces their phosphorylation [ 12 ] . They also suggest that the YQXP motifs may be involved in binding to other intracellular signaling molecules.

  • The v-crk SH2 domain interacts with YXXP motifs upon phosphorylation, suggesting that both of these regions may be able to interact with v-crk [ 37 ] . Fusions of the kinase inactive Src kinase domain and either the full Cas SD, the 5' region of the Cas SD (Cas(5'SD), containing 4 YQXP motifs) or the 3' of the Cas SD (Cas(3'SD), containing 9 YDXP motifs), are not stably tyrosine phosphorylated when expressed alone in cells (data not shown and see Fig.

  • Using different regions of the Cas SD containing either the YDXP or the YQXP motifs, we could demonstrate that v-crk specifically interacts with the C-terminal YDXP motifs when tyrosine phosphorylated.

  • Since crk is the major protein reported to bind to the Cas SD, our data suggest that the YQXP motifs may interact with other yet to be identified downstream effectors.


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