Whether YAP1 induction and decreased p21, in that context, would influence the HSC pool remains to be investigated. While our findings indicate that YAP1 does not affect HSC function, it is possible that a downstream mediator of the Hippo pathway, other than Yap1, is active in hematopoietic cells. In Drosophila, the Yap1 homolog Yorkie is the only known effector in the Hippo pathway. In mammalian cells, however, the evolutionary divergent Yap1 paralog Taz has partially overlapping functions with Yap1, forming complexes with TEAD transcription factors and mediates cell proliferation. It has, however, been demonstrated that Yap and Taz has several distinct functions that are dependent on species and tissue type. Consequently, it would be interesting to investigate whether Taz has an active role in regulation of hematopoeisis and HSCs. Indeed, our preliminary observations suggest that Taz is expressed at relatively high levels within the LT-HSC compartment but not in progenitors and differentiated hematopoietic cells. In summary, our findings conclusively show that counteracting Hippo signaling by enforced YAP1 expression does not alter in vivo hematopoiesis or HSC function. More work will be required to elucidate whether other aspects of Hippo signaling, directly or Salvianolic-acid-B indirectly, may influence hematopoietic cells, either through the Yap paralog Taz, or through actions on neighboring nonhematopoietic cells in the bone marrow microenvironment. Although there is a consensus that the NMDA receptor forms a hetero-tetramer with subunits arranged as a dimer-of -dimers, the subunit arrangement within a dimer and the organization of the two dimers are under debate. Two possible arrangements have been proposed. On the one hand, experiments utilizing fluorescence resonance energy transfer measurements with fluorophore-tagged subunits and cysteine knockout mutants of GluN1 were interpreted in terms of a dimer of homodimers. On the other hand, the crystal structure of a GluN1/GluN2A LBD heterodimer, FRET measurements with fluorophore-tagged LBDs, and studies on GluN3 subunits are consistent with a dimer-of-heterodimer configuration. To probe the arrangement of NMDA receptor subunits within a dimer, and to resolve the controversy of homodimer versus heterodimer, we studied the association of subunits at the level of the ATD using cysteine-directed chemical cross-linking. Importantly, experiments by other groups have shown that GluN1 C79A and C308A mutants coexpressed with GluN2A traffic to the cell membranes, form functional receptors and do not affect receptor oligomerization. Thus, the reason why we did not observe the formation of disulfide bond-mediated dimers with GluN1 C79A C308A double mutant is not due to the impairment of subunit expression, trafficking or assembly. The GluN1 ATD has been proposed to mask the retention signal on the GluN2A ATD, a conclusion that is in line with the heteromeric interaction of their respective ATDs. Our results may also explain why the isolated GluN2B ATD predominately exists as a monomer when the GluN1 ATD was not coexpressed. In fact, the isolated GluN2 ATD could associate with the isolated GluN1 ATD in solution. On the other hand, several studies have shown that full-length GluN1 subunits or isolated GluN1 domains, when expressed alone, could form homodimers. This has been used as an argument supporting the dimer-of-homodimer model for NMDA receptor. In the present study, upon expression of the GluN1 subunit alone, we also detected a weak band with a size Atropine sulfate approximately commensurate with a GluN1 homodimer.