Figure 1.
ROR1 signaling. The structure of ROR1 is provided with each of the various domains labeled in red font to the right or left of the ROR1 stick figure, marking the extracellular immunoglobulinlike domain, CRD, and Kringle domain and the intracellular tyrosine kinase–like domain, the serine/threonine-rich domains, and the proline-rich domain (PRD). The binding of Wnt5a to the CRD can trigger activation of ROR1 signaling with recruitment and activation of cytosolic accessory molecules in green rectangles via defined (solid arrows) or speculated (dashed arrows) signaling pathways, culminating in the expression of ERK1/2, NF-kB, and NRF2 target genes in the nucleus. Red rectangles delineate inactive or inhibitory signaling molecules. Small circles labeled P represent protein phosphorylation.

ROR1 signaling. The structure of ROR1 is provided with each of the various domains labeled in red font to the right or left of the ROR1 stick figure, marking the extracellular immunoglobulinlike domain, CRD, and Kringle domain and the intracellular tyrosine kinase–like domain, the serine/threonine-rich domains, and the proline-rich domain (PRD). The binding of Wnt5a to the CRD can trigger activation of ROR1 signaling with recruitment and activation of cytosolic accessory molecules in green rectangles via defined (solid arrows) or speculated (dashed arrows) signaling pathways, culminating in the expression of ERK1/2, NF-kB, and NRF2 target genes in the nucleus. Red rectangles delineate inactive or inhibitory signaling molecules. Small circles labeled P represent protein phosphorylation.

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