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It has been reported that the N-terminus of DAT is essential for protein kinase C-mediated phosphorylation on serine residues [67], and the first 22 amino acids from the N-terminus of DAT eliminate phosphorylation of DAT in response to PKC activation [44]

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The peptide acts directly on fibroblasts at the repair site, and patients with tendinopathy generally report noticeable reduction in localized pain and improved range of motion within that window

The authors demonstrate elegantly that changes in substrate stiffness can coordinate morphogenesis by triggering collective cell migration and promoting EMT in vivo