RMDN3
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| RMDN3 | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Aliases | RMDN3, FAM82A2, FAM82C, RMD-3, RMD3, ptpip51, regulator of microtubule dynamics 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 611873; MGI: 1915059; HomoloGene: 34926; GeneCards: RMDN3; OMA:RMDN3 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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Regulator of microtubule dynamics protein 3 (RMDN3), more commonly known as Protein tyrosine phosphatase interacting protein 51 (PTPIP51), is a protein that in humans is encoded by the RMDN3 gene on chromosome 15.[5][6] This protein contributes to multiple biological functions, including cellular differentiation, proliferation, motility, cytoskeleton formation, and apoptosis, and has been associated with numerous cancers.[7][8][9]
PTPIP51 contains two conserved domains, called conserved region 1 (CR1) and conserved region 2 (CR2), which serve as binding sites for 14-3-3 proteins. Close to these conserved domains are two tyrosine residues, tyrosine 53 and 158, which serve as phosphorylation sites for various kinases.[8] In addition, PTPIP51 has a mitochondrial targeting sequence at its N-terminal which is responsible for inducing apoptosis, though some splicing variants lack this sequence.[5][10] It also contains a 33-residue coiled coil domain at positions 92 – 124.[5] Crystal structure of TPR domain of PTPIP51 was determined.[11]
Function
PTPIP51 is a member of the RMDN protein family and localizes to the outer mitochondrial membrane, cytoplasm, and nucleus.[5] This protein is involved in cellular differentiation, proliferation, motility, cytoskeleton formation, and apoptosis.[7][8] These biological functions thus serve to facilitate mammalian development through processes such as placental villi formation and angiogenesis.[7][10] In particular, it is expressed in differentiated cells and tissues, such as follicular and inter-follicular epidermis, epithelia, skeletal muscle, testis, and nervous tissue.[7][10] PTPIP51 is also expressed differentially in neutrophils, but not other immune cells, and thus may partake in immune cell signaling and myeloid development by interacting with TCPTP and PTP1B.[10] Its interactions with PTP1B, along with the proteins 14-3-3β, Raf-1, c-Src, PKA, and DAGKα, determine the mechanisms by which it influences the mitogen-activated protein kinase (MAPK) pathway.[8] PTPIP51 has been observed to induce apoptosis by disrupting the mitochondrial membrane potential, resulting in the release of cytochrome c.[12] In vitro phospholipid binding and transfer functions has been reported [11]