IndraLab

Statements


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"While the human DOPEY2 appears not to be functionally required for MON2-dependent sorting of HA-Wls, the MON2-PAD1 complex in C. elegans is required for in vivo Wnt morphogenic gradient formation."

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"Together, these data provide evidence of a genetic linkage between SNX3-retromer and the MON-2-PAD-1 complex in this process."

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"Taken together, these results are consistent with a requirement of the MON2-PAD-1 complex and the putative flippase activity of TAT5 in the in vivo SNX3-retromer-mediated Wls retrieval and Wnt secretion in C. elegans."

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"Building on evidence from yeast , we therefore propose a working model (Fig. 5f) in which TAT5/ATP9A and the MON2-PAD1 complex are associated with SNX3-retromer on the endosomal network."

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"phosphatidylethanolamine), provides an environment for the membrane recruitment and assembly of coat proteins and other accessory factors, including the MON2-PAD1 complex, that aid formation of vesicular transport carriers."

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"Testing aspects of this model and how it has functionally evolved from yeast to humans will provide further mechanistic details of SNX3-retromer mediated sorting and elucidate the role of the MON2-PAD1 complex as an evolutionary conserved endosomal coat, and, more broadly, the role of flippases in carrier formation during membrane transport.In C. elegans, the retromer-dependent sorting of the bone morphogenetic protein (BMP) type I receptor, SMA-6, is also severely perturbed in mutants of Ce-snx-3 but not snx-1 or Ce-snx-27 ."