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- W2090552013 abstract "The EMBO conference/FEBS advanced course, ‘Europhosphatases Conference 2005’, on The Biology of Phosphatases, was held in Churchill College, Cambridge University, UK, between 10 and 14 July 2005. The conference was organized by D. Alexander, J. Arino and E. Da Cruz e Silva.![][1] “Now is not the end. It is not even the beginning of the end. But it is, perhaps, the end of the beginning”. This quotation from Sir Winston Churchill had resonance at the recent ‘Europhosphatases Conference 2005’ held at Churchill College, Cambridge. Although the identity of each of the protein phosphatase genes in the human genome is now known, the challenges of determining the enzymes' interacting partners, mechanisms of regulation, physiological substrates, biological roles and their links to disease remain substantial. The timing of the conference was particularly opportune because 2005 marked the 50th anniversary of the seminal discovery, by Edmond Fischer and Edwin Krebs, of reversible protein phosphorylation—a control mechanism now appreciated to pervade all aspects of cell physiology. In this overview of the meeting, we describe the current status of the protein phosphatase field and highlight some of the emerging themes.Unlike protein kinases, which derive from a common ancestor, protein phosphatases have evolved from distinct progenitors and therefore have no common co‐factor requirements and no shared structural features. Protein phosphatases were originally characterized as hydrolysing phosphoryl groups from proteins, but it is now understood that a limited number of protein phosphatases have the capacity to remove phosphate from either phospholipids or mRNA. Protein phosphatases can be broadly classified, on the basis of their structure, into the PPP and PPM families (Barford, 1996), which dephosphorylate phosphoserine (pSer) and phosphothreonine (pThr), and into the cysteine‐based PTPs, most of which dephosphorylate either phosphotyrosine (pTyr) exclusively or pTyr and pThr. The catalytic mechanism for the protein phosphatases involves a … [1]: /embed/graphic-1.gif" @default.
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- W2090552013 title "The whys and wherefores of phosphate removal" @default.
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- W2090552013 doi "https://doi.org/10.1038/sj.embor.7400644" @default.
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!["The EMBO conference/FEBS advanced course, ‘Europhosphatases Conference 2005’, on The Biology of Phosphatases, was held in Churchill College, Cambridge University, UK, between 10 and 14 July 2005. The conference was organized by D. Alexander, J. Arino and E. Da Cruz e Silva.![][1] “Now is not the end. It is not even the beginning of the end. But it is, perhaps, the end of the beginning”. This quotation from Sir Winston Churchill had resonance at the recent ‘Europhosphatases Conference 2005’ held at Churchill College, Cambridge. Although the identity of each of the protein phosphatase genes in the human genome is now known, the challenges of determining the enzymes' interacting partners, mechanisms of regulation, physiological substrates, biological roles and their links to disease remain substantial. The timing of the conference was particularly opportune because 2005 marked the 50th anniversary of the seminal discovery, by Edmond Fischer and Edwin Krebs, of reversible protein phosphorylation—a control mechanism now appreciated to pervade all aspects of cell physiology. In this overview of the meeting, we describe the current status of the protein phosphatase field and highlight some of the emerging themes.Unlike protein kinases, which derive from a common ancestor, protein phosphatases have evolved from distinct progenitors and therefore have no common co‐factor requirements and no shared structural features. Protein phosphatases were originally characterized as hydrolysing phosphoryl groups from proteins, but it is now understood that a limited number of protein phosphatases have the capacity to remove phosphate from either phospholipids or mRNA. Protein phosphatases can be broadly classified, on the basis of their structure, into the PPP and PPM families (Barford, 1996), which dephosphorylate phosphoserine (pSer) and phosphothreonine (pThr), and into the cysteine‐based PTPs, most of which dephosphorylate either phosphotyrosine (pTyr) exclusively or pTyr and pThr. The catalytic mechanism for the protein phosphatases involves a … [1]: /embed/graphic-1.gif"](?object=%22The%20EMBO%20conference%2FFEBS%20advanced%20course%2C%20%E2%80%98Europhosphatases%20Conference%202005%E2%80%99%2C%20on%20The%20Biology%20of%20Phosphatases%2C%20was%20held%20in%20Churchill%20College%2C%20Cambridge%20University%2C%20UK%2C%20between%2010%20and%2014%20July%202005.%20The%20conference%20was%20organized%20by%20D.%20Alexander%2C%20J.%20Arino%20and%20E.%20Da%20Cruz%20e%20Silva.!%5B%5D%5B1%5D%20%E2%80%9CNow%20is%20not%20the%20end.%20It%20is%20not%20even%20the%20beginning%20of%20the%20end.%20But%20it%20is%2C%20perhaps%2C%20the%20end%20of%20the%20beginning%E2%80%9D.%20This%20quotation%20from%20Sir%20Winston%20Churchill%20had%20resonance%20at%20the%20recent%20%E2%80%98Europhosphatases%20Conference%202005%E2%80%99%20held%20at%20Churchill%20College%2C%20Cambridge.%20Although%20the%20identity%20of%20each%20of%20the%20protein%20phosphatase%20genes%20in%20the%20human%20genome%20is%20now%20known%2C%20the%20challenges%20of%20determining%20the%20enzymes'%20interacting%20partners%2C%20mechanisms%20of%20regulation%2C%20physiological%20substrates%2C%20biological%20roles%20and%20their%20links%20to%20disease%20remain%20substantial.%20The%20timing%20of%20the%20conference%20was%20particularly%20opportune%20because%202005%20marked%20the%2050th%20anniversary%20of%20the%20seminal%20discovery%2C%20by%20Edmond%20Fischer%20and%20Edwin%20Krebs%2C%20of%20reversible%20protein%20phosphorylation%E2%80%94a%20control%20mechanism%20now%20appreciated%20to%20pervade%20all%20aspects%20of%20cell%20physiology.%20In%20this%20overview%20of%20the%20meeting%2C%20we%20describe%20the%20current%20status%20of%20the%20protein%20phosphatase%20field%20and%20highlight%20some%20of%20the%20emerging%20themes.Unlike%20protein%20kinases%2C%20which%20derive%20from%20a%20common%20ancestor%2C%20protein%20phosphatases%20have%20evolved%20from%20distinct%20progenitors%20and%20therefore%20have%20no%20common%20co%E2%80%90factor%20requirements%20and%20no%20shared%20structural%20features.%20Protein%20phosphatases%20were%20originally%20characterized%20as%20hydrolysing%20phosphoryl%20groups%20from%20proteins%2C%20but%20it%20is%20now%20understood%20that%20a%20limited%20number%20of%20protein%20phosphatases%20have%20the%20capacity%20to%20remove%20phosphate%20from%20either%20phospholipids%20or%20mRNA.%20Protein%20phosphatases%20can%20be%20broadly%20classified%2C%20on%20the%20basis%20of%20their%20structure%2C%20into%20the%20PPP%20and%20PPM%20families%20(Barford%2C%201996)%2C%20which%20dephosphorylate%20phosphoserine%20(pSer)%20and%20phosphothreonine%20(pThr)%2C%20and%20into%20the%20cysteine%E2%80%90based%20PTPs%2C%20most%20of%20which%20dephosphorylate%20either%20phosphotyrosine%20(pTyr)%20exclusively%20or%20pTyr%20and%20pThr.%20The%20catalytic%20mechanism%20for%20the%20protein%20phosphatases%20involves%20a%20%E2%80%A6%20%5B1%5D%3A%20%2Fembed%2Fgraphic-1.gif%22){kind=link}