@misc{CencilNitschkeSteupetal.2014,
  author    = {Cencil, Ugo and Nitschke, Felix and Steup, Martin and Minassian, Berge A. and Colleoni, Christophe and Ball, Steven G.},
  title     = {Transition from glycogen to starch metabolism in Archaeplastida},
  series = {Trends in plant science},
  volume    = {19},
  journal   = {Trends in plant science},
  number    = {1},
  publisher = {Elsevier},
  address   = {London},
  issn      = {1360-1385},
  doi       = {10.1016/j.tplants.2013.08.004},
  pages     = {18 -- 28},
  year      = {2014},
  abstract  = {In this opinion article we propose a scenario detailing how two crucial components have evolved simultaneously to ensure the transition of glycogen to starch in the cytosol of the Archaeplastida last common ancestor: (i) the recruitment of an enzyme from intracellular Chlamydiae pathogens to facilitate crystallization of alpha-glucan chains; and (ii) the evolution of novel types of polysaccharide (de)phosphorylating enzymes from preexisting glycogen (de)phosphorylation host pathways to allow the turnover of such crystals. We speculate that the transition to starch benefitted Archaeplastida in three ways: more carbon could be packed into osmotically inert material; the host could resume control of carbon assimilation from the chlamydial pathogen that triggered plastid endosymbiosis; and cyanobacterial photosynthate export could be integrated in the emerging Archaeplastida.},
  language  = {en}
}
@misc{SullivanNitschkeSteupetal.2017,
  author    = {Sullivan, Mitchell A. and Nitschke, Silvia and Steup, Martin and Minassian, Berge A. and Nitschke, Felix},
  title     = {Pathogenesis of Lafora disease},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {1080},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-47462},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-474622},
  pages     = {18},
  year      = {2017},
  abstract  = {Lafora disease (LD, OMIM \#254780) is a rare, recessively inherited neurodegenerative disease with adolescent onset, resulting in progressive myoclonus epilepsy which is fatal usually within ten years of symptom onset. The disease is caused by loss-of-function mutations in either of the two genes EPM2A (laforin) or EPM2B (malin). It characteristically involves the accumulation of insoluble glycogen-derived particles, named Lafora bodies (LBs), which are considered neurotoxic and causative of the disease. The pathogenesis of LD is therefore centred on the question of how insoluble LBs emerge from soluble glycogen. Recent data clearly show that an abnormal glycogen chain length distribution, but neither hyperphosphorylation nor impairment of general autophagy, strictly correlates with glycogen accumulation and the presence of LBs. This review summarizes results obtained with patients, mouse models, and cell lines and consolidates apparent paradoxes in the LD literature. Based on the growing body of evidence, it proposes that LD is predominantly caused by an impairment in chain-length regulation affecting only a small proportion of the cellular glycogen. A better grasp of LD pathogenesis will further develop our understanding of glycogen metabolism and structure. It will also facilitate the development of clinical interventions that appropriately target the underlying cause of LD.},
  language  = {en}
}
@article{NitschkeWangSchmiederetal.2013,
  author    = {Nitschke, Felix and Wang, Peixiang and Schmieder, Peter and Girard, Jean-Marie and Awrey, Donald E. and Wang, Tony and Israelian, Johan and Zhao, XiaoChu and Turnbull, Julie and Heydenreich, Matthias and Kleinpeter, Erich and Steup, Martin and Minassian, Berge A.},
  title     = {Hyperphosphorylation of glucosyl C6 carbons and altered structure of glycogen in the neurodegenerative epilepsy lafora disease},
  series = {Cell metabolism},
  volume    = {17},
  journal   = {Cell metabolism},
  number    = {5},
  publisher = {Cell Press},
  address   = {Cambridge},
  issn      = {1550-4131},
  doi       = {10.1016/j.cmet.2013.04.006},
  pages     = {756 -- 767},
  year      = {2013},
  abstract  = {Laforin or malin deficiency causes Lafora disease, characterized by altered glycogen metabolism and teenage-onset neurodegeneration with intractable and invariably fatal epilepsy. Plant starches possess small amounts of metabolically essential monophosphate esters. Glycogen contains similar phosphate amounts, which are thought to originate from a glycogen synthase error side reaction and therefore lack any specific function. Glycogen is also believed to lack monophosphates at glucosyl carbon C6, an essential phosphorylation site in plant starch metabolism. We now show that glycogen phosphorylation is not due to a glycogen synthase side reaction, that C6 is a major glycogen phosphorylation site, and that C6 monophosphates predominate near centers of glycogen molecules and positively correlate with glycogen chain lengths. Laforin or malin deficiency causes C6 hyperphosphorylation, which results in malformed long-chained glycogen that accumulates in many tissues, causing neurodegeneration in brain. Our work advances the understanding of Lafora disease pathogenesis and suggests that glycogen phosphorylation has important metabolic function.},
  language  = {en}
}