Abstract
Post-translational modifications (PTMs) of proteins regulate self-renewal and differentiation in embryonic stem cells (ESCs). Nitration of tyrosine residues of proteins in ESCs modulates their downstream pathways, which can affect self-renewal and differentiation. However, protein tyrosine nitration (PTN) in ESCs has been rarely studied. We reviewed 23 nitrated sites in stem cell proteins. Functional enrichment analysis showed that these nitrated proteins are involved in signal transduction, cell adhesion and migration, and cell proliferation in ESCs. Comparison between the nitrated and known phosphorylated sites revealed that 7 nitrated sites had overlapping phosphorylated sites, indicating functional links of PTNs to their associated signaling pathways in ESCs. Therefore, nitrated proteome provides a basis for understanding potential roles of PTN in self-renewal and differentiation of ESCs.
Highlights
Nitration of tyrosine residues modulates the activity of proteins, thereby affecting their downstream processes.[1]
Nitrated proteome provides a basis for understanding potential roles of protein tyrosine nitration (PTN) in self-renewal and differentiation of embryonic stem cells (ESCs)
A growing body of evidence suggests that PTN can play roles in self-renewal and differentiation of embryonic stem cells (ESCs)[4,5,6,7,8,9] during early embryogenesis, nitric oxide (NO) synthases are expressed in the growing embryo, implying the presence of reactive nitrogen species (RNS) gradients in the developing organs.[10,11,12]
Summary
Abstract : Post-translational modifications (PTMs) of proteins regulate self-renewal and differentiation in embryonic stem cells (ESCs). Nitration of tyrosine residues of proteins in ESCs modulates their downstream pathways, which can affect self-renewal and differentiation. Protein tyrosine nitration (PTN) in ESCs has been rarely studied. We reviewed 23 nitrated sites in stem cell proteins. Functional enrichment analysis showed that these nitrated proteins are involved in signal transduction, cell adhesion and migration, and cell proliferation in ESCs. Comparison between the nitrated and known phosphorylated sites revealed that 7 nitrated sites had overlapping phosphorylated sites, indicating functional links of PTNs to their associated signaling pathways in ESCs. nitrated proteome provides a basis for understanding potential roles of PTN in self-renewal and differentiation of ESCs. Keywords : Tyrosine nitration, Nitrotyrosine enrichment, LC-MS/MS, Proteomics, Embryonic stem cells
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