IA-2 (also known as PTPRN or ICA512) and phogrin (also known as PTPRN2, IA-2b, IAR or ICAAR) are homologous protein-tyrosine phosphatase (PTP) receptors. They have a signal peptide, an ectodomain, a single-pass transmembrane region, and a single intracellular PTP domain. Processing of pro IA-2 by furin-like hormone convertases produces mature IA-2, which lacks the signal peptide and an adjacent fragment (residues 1-448). Upon exocytosis, the cytoplasmic domain of IA-2 is cleaved and moves to the nucleus where it enhances transcription of the insulin gene []. The mature ectodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolysed in vitro by reactive oxygen species, which may be anew shedding mechanism [].
IA-2 (also known as PTPRN or ICA512) and phogrin (also known as PTPRN2, IA-2b, IAR or ICAAR) are homologous protein-tyrosine phosphatase (PTP) receptors. They have a signal peptide, an ectodomain, a single-pass transmembrane region, and a single intracellular PTP domain. Processing of pro IA-2 by furin-like hormone convertases produces mature IA-2, which lacks the signal peptide and an adjacent fragment (residues 1-448). Upon exocytosis, the cytoplasmic domain of IA-2 is cleaved and moves to the nucleus where it enhances transcription of the insulin gene []. The mature ectodomain of IA-2 participates in adhesion to the extracellular matrix and is self-proteolysed in vitro by reactive oxygen species, which may be a new shedding mechanism [].
