journal article
LitStream Collection
doi: 10.1002/bies.201090061pmid: N/A
Cover Photograph: Hypothetical structure of the dynamin oligomer. During endocytosis clathrincoated pits and ultimately vesicles are formed at the plasma membrane. The constriction and cleavage of these vesicles is achieved by the action of the GTPase dynamin. On pages 1033–1039 Nikolaus Pawlowski discusses recent findings on the structure and function of dynamin and explains how dynamin oligomers are expected to form and thus participate in vesicle fission. The oligomerisation of two other dynamin superfamily proteins is also briefly addressed. (Structure as suggested by Gao et al., Nature 465: 502‐6.)
Joulie, Michael; Miotto, Benoit; Defossez, Pierre‐Antoine
doi: 10.1002/bies.201000057pmid: 20886526
CpG islands (CGIs) are regions enriched in the dinucleotide CpG; they constitute the promoter of about 60% of mammalian genes. In cancer cells, some promoter‐associated CGIs become heavily methylated on cytosines, and the corresponding genes undergo stable transcriptional silencing. Hypermethylated CGIs attract methyl‐CpG‐binding proteins (MBPs), which have been shown to recruit chromatin modifiers and cause transcriptional repression. These observations have led to the prevalent model that methyl‐CpG‐binding proteins are promoter‐proximal transcriptional repressors. Recent discoveries challenge this idea and raise a number of questions. Here we discuss the following issues: what are other possible roles for the known MBPs? Why are these proteins not essential in mammals? Are there other MBPs left to discover? Could CpG methylation be nonessential?
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