Render Target: STATIC
Render Timestamp: 2025-03-14T10:26:29.242Z
Commit: a619ae74f66dae0f27639e88da12bcf600e46428
XML generation date: 2025-03-11 22:02:16.771
Product last modified at: 2025-03-13T08:00:11.765Z
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PDP - Template Name: Antibody Duet
PDP - Template ID: *******ad0fa02

PhosphoPlus® YAP (Ser61) Antibody Duet #85629

    Product Information

    Product Description

    PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.

    Background

    YAP (Yes-associated protein, YAP65) was first identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size (6-8). Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (7-9). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteasomal degradation of YAP (10).
    YAP function is influenced by cellular metabolic status. This was recognized after observing that AMPK, a master regulator of cell metabolism, directly phosphorylates YAP at multiple sites (e.g., Ser61, Ser94) during energy stress or nutritional deprivation (11-13). Phosphorylation of Ser61 by AMPK did not increase 14-3-3 binding or affect YAP subcellular localization, but nevertheless resulted in transcriptional repression of YAP target genes (12).
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