TAILIEUCHUNG - Báo cáo khoa học: Protein tyrosine phosphatases: sequences and beyond

The 21st century is bringing a flood of genomic sequence data from diverse species and although this information is highly accessible, we are far from understanding its content. Recent discoveries, for example on novel RNA types, clearly show that there is still much to learn. | IFEBS Journal MINIREVIEW SERIES Protein tyrosine phosphatases sequences and beyond Wiljan J. A. J. Hendriks1 and Andrew W. Stoker2 1 Radboud University Nijmegen MedicalCentre the Netherlands 2 UCL Institute of Child Health London UK The 21st century is bringing a flood of genomic sequence data from diverse species and although this information is highly accessible we are far from understanding its content. Recent discoveries for example on novel RNA types clearly show that there is still much to learn. In addition the many often reversible post-translational modifications imposed upon RNAs and proteins are difficult to extract from these primary sequence data. Powers to predict such modification-prone sites are currently very modest but at least we are now able to list the modifying enzymes involved. The future challenge is to elucidate the structure-function relationships the imposed regulatory mechanisms and the contributions to health and disease for these post-translational modifiers. Phosphorylation on tyrosine residues is one key post-translational modification that cells use to control protein function especially in cellular signalling pathways. The extent of tyrosine phosphorylation is dictated by the balance of activities of protein tyrosine kinases and protein tyrosine phosphatases PTPs . Since purification of the first PTP in 1988 a wide variety of PTPs has been discovered by exploiting their well-conserved PTP signature motif HCX5R encompassing the catalytic site cysteine . The human PTP family contains 107 members of which 38 belong to the phosphotyrosine-specific classical PTP subfamily and 61 to the so-called dual-specific phosphatases DUSPs . The latter can also dephosphorylate serine and threonine residues and even phospholipids. The exceptionally high enzyme activity and notorious sub strate promiscuity displayed by PTPs in vitro have often confounded research concerning their signalling roles. Recent use of animal models and state-of-the-art .

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