{"title":"Cellular and molecular mechanics of gliding locomotion in eukaryotes.","authors":"Matthew B Heintzelman","doi":"10.1016/S0074-7696(06)51003-4","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)51003-4","url":null,"abstract":"<p><p>Gliding is a form of substrate-dependent cell locomotion exploited by a variety of disparate cell types. Cells may glide at rates well in excess of 1 microm/sec and do so without the gross distortion of cellular form typical of amoeboid crawling. In the absence of a discrete locomotory organelle, gliding depends upon an assemblage of molecules that links cytoplasmic motor proteins to the cell membrane and thence to the appropriate substrate. Gliding has been most thoroughly studied in the apicomplexan parasites, including Plasmodium and Toxoplasma, which employ a unique assortment of proteins dubbed the glideosome, at the heart of which is a class XIV myosin motor. Actin and myosin also drive the gliding locomotion of raphid diatoms (Bacillariophyceae) as well as the intriguing form of gliding displayed by the spindle-shaped cells of the primitive colonial protist Labyrinthula. Chlamydomonas and other flagellated protists are also able to abandon their more familiar swimming locomotion for gliding, during which time they recruit a motility apparatus independent of that driving flagellar beating.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"251 ","pages":"79-129"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)51003-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26227328","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Biology of Langerhans cells and Langerhans cell histiocytosis.","authors":"G I Bechan, R M Egeler, R J Arceci","doi":"10.1016/S0074-7696(06)54001-X","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)54001-X","url":null,"abstract":"<p><p>Langerhans cells (LC) are epidermal dendritic cells (DC). They play an important role in the initiation of immune responses through antigen uptake, processing, and presentation to T cells. Langerhans cell histiocytosis (LCH) is a rare disease in which accumulation of cells with LC characteristics (LCH cells) occur. LCH lesions are further characterized by the presence of other cell types, such as T cells, multinucleated giant cells (MGC), macrophages (MPhi), eosinophils, stromal cells, and natural killer cells (NK cells). Much has been learned about the pathophysiology of LCH by studying properties of these different cells and their interaction with each other through cytokines/chemokines. In this review we discuss the properties and interactions of the different cells involved in LCH pathophysiology with the hope of better understanding this enigmatic disorder.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"254 ","pages":"1-43"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)54001-X","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26424522","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tsuyoshi Mizoguchi, Johanna Putterill, Yuri Ohkoshi
{"title":"Kinase and phosphatase: the cog and spring of the circadian clock.","authors":"Tsuyoshi Mizoguchi, Johanna Putterill, Yuri Ohkoshi","doi":"10.1016/S0074-7696(06)50002-6","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)50002-6","url":null,"abstract":"<p><p>Reversible phosphorylation is an important regulatory mechanism for many biological processes in eukaryotic organisms. The phosphorylation state of a protein is controlled dynamically by both protein kinases and phosphatases. Phosphorylation of circadian clock proteins is an essential posttranscriptional mechanism in the regulation of circadian clocks, and several protein kinases and phosphatases have been shown to regulate key clock components in eukaryotic systems, including Arabidopsis, Neurospora, Drosophila, and mice. In this review, recent progress in the characterization of protein kinases and phosphatases involved in circadian rhythms is summarized. The protein kinase CK2 has been proposed as an evolutionary link between the divergent circadian systems of plants, animals, and fungi. The roles of CK2 in this process are discussed here in detail.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"250 ","pages":"47-72"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)50002-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26157430","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Sergei I Grivennikov, Dmitry V Kuprash, Zheng-Gang Liu, Sergei A Nedospasov
{"title":"Intracellular signals and events activated by cytokines of the tumor necrosis factor superfamily: From simple paradigms to complex mechanisms.","authors":"Sergei I Grivennikov, Dmitry V Kuprash, Zheng-Gang Liu, Sergei A Nedospasov","doi":"10.1016/S0074-7696(06)52002-9","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)52002-9","url":null,"abstract":"<p><p>Tumor necrosis factor (TNF) and several related cytokines can induce opposite effects such as cell activation and proliferation or cell death. How the cell maintains the balance between these seemingly mutually exclusive pathways has long remained a mystery. TNF receptor I (TNFRI) initially emerged as a potent activator of NFkappaB and AP-1 transcription factors, while the related CD95 (Fas, Apo-1) was recognized as a prototype death receptor. Advances in research have uncovered critical molecular players in these intracellular processes. They have also revealed a much more complex picture than originally thought. Several new signaling pathways, including the alternative NFkappaB activation cascade, have been uncovered, and previously unknown modes of cross-talk between intracellular signaling molecules were revealed. It also turned out that signaling mechanisms mediated by the TNF receptor superfamily members can operate not only in the immune system but also in organ development.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"252 ","pages":"129-61"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)52002-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26260881","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Role of peripherin/rds in vertebrate photoreceptor architecture and inherited retinal degenerations.","authors":"Andrew F X Goldberg","doi":"10.1016/S0074-7696(06)53004-9","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)53004-9","url":null,"abstract":"<p><p>The vertebrate photoreceptor outer segment (OS) is a highly structured and dynamic organelle specialized to transduce light signals. The elaborate membranous architecture of the OS requires peripherin/rds (P/rds), an integral membrane protein and tetraspanin protein family member. Gene-level defects in P/rds cause a broad variety of late-onset progressive retinal degenerations in humans and dysmorphic photoreceptors in murine and Xenopus models. Although proposed to fulfill numerous roles related to OS structural stability and renewal, P/rds molecular function remains uncertain. An increasingly resolved model of this protein's oligomeric structure can account for disease inheritance patterns and severity in some instances. Nonetheless, the pathogenic mechanisms underlying the uniquely broad spectrum of retinal diseases associated with P/rds defects are not currently well understood. Recent findings point to the possibility that P/rds acts as a multifunctional scaffolding protein for OS architecture and that partial-loss-of-function mutations contribute to the hallmark phenotypic heterogeneity associated with inherited defects in RDS.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"253 ","pages":"131-75"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)53004-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26358135","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Geurt Schilders, Erwin van Dijk, Reinout Raijmakers, Ger J M Pruijn
{"title":"Cell and molecular biology of the exosome: how to make or break an RNA.","authors":"Geurt Schilders, Erwin van Dijk, Reinout Raijmakers, Ger J M Pruijn","doi":"10.1016/S0074-7696(06)51005-8","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)51005-8","url":null,"abstract":"<p><p>The identification and characterization of the exosome complex has shown that the exosome is a complex of 3' --> 5' exoribonucleases that plays a key role in the processing and degradation of a wide variety of RNA substrates. Advances in the understanding of exosome function have led to the identification of numerous cofactors that are required for a selective recruitment of the exosome to substrate RNAs, for their structural alterations to facilitate degradation, and to aid in their complete degradation/processing. Structural data obtained by two-hybrid interaction analyses and X-ray crystallography show that the core of the exosome adopts a doughnut-like structure and demonstrates that probably not all exosome subunits are active exoribonucleases. Despite all data obtained on the structure and function of the exosome during the last decade, there are still a lot of unanswered questions. What is the molecular mechanism by which cofactors select and target substrate RNAs to the exosome and modulate its function for correct processing or degradation? How can the exosome discriminate between processing or degradation of a specific substrate RNA? What is the precise structure of exosome subunits and how do they contribute to its function? Here we discuss studies that provide some insight to these questions and speculate on the mechanisms that control the exosome.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"251 ","pages":"159-208"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)51005-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26227330","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Elison B Blancaflor, Yuh-Shuh Wang, Christy M Motes
{"title":"Organization and function of the actin cytoskeleton in developing root cells.","authors":"Elison B Blancaflor, Yuh-Shuh Wang, Christy M Motes","doi":"10.1016/S0074-7696(06)52004-2","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)52004-2","url":null,"abstract":"<p><p>The actin cytoskeleton is a highly dynamic structure, which mediates various cellular functions in large part through accessory proteins that tilt the balance between monomeric G-actin and filamentous actin (F-actin) or by facilitating interactions between actin and the plasma membrane, microtubules, and other organelles. Roots have become an attractive model to study actin in plant development because of their simple anatomy and accessibility of some root cell types such as root hairs for microscopic analyses. Roots also exhibit a remarkable developmental plasticity and possess a delicate sensory system that is easily manipulated, so that one can design experiments addressing a range of important biological questions. Many facets of root development can be regulated by the diverse actin network found in the various root developmental regions. Various molecules impinge on this actin scaffold to define how a particular root cell type grows or responds to a specific environmental signal. Although advances in genomics are leading the way toward elucidating actin function in roots, more significant strides will be realized when such tools are combined with improved methodologies for accurately depicting how actin is organized in plant cells.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"252 ","pages":"219-64"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)52004-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26260883","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Adaptations for nocturnal vision in insect apposition eyes.","authors":"Birgit Greiner","doi":"10.1016/S0074-7696(06)50001-4","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)50001-4","url":null,"abstract":"<p><p>Due to our own preference for bright light, we tend to forget that many insects are active in very dim light. Nocturnal insects possess in general superposition compound eyes. This eye design is truly optimized for dim light as photons can be gathered through large apertures comprised of hundreds of lenses. In apposition eyes, on the other hand, the aperture consists of a single lens resulting in a poor photon catch and unreliable vision in dim light. Apposition eyes are therefore typically found in day-active insects. Some nocturnal insects have nevertheless managed the transition to a strictly nocturnal lifestyle while retaining their highly unsuitable apposition eye design. Large lenses and wide photoreceptors enhance the sensitivity of nocturnal apposition eyes. However, as the gain of these optical adaptations is limited and not sufficient for vision in dim light, additional neural adaptations in the form of spatial and temporal summation are necessary.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"250 ","pages":"1-46"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)50001-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26157429","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"New insights into nucleolar architecture and activity.","authors":"Ivan Raska, Peter J Shaw, Dusan Cmarko","doi":"10.1016/S0074-7696(06)55004-1","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)55004-1","url":null,"abstract":"<p><p>The nucleolus is the most obvious and clearly differentiated nuclear subcompartment. It is where ribosome biogenesis takes place and has been the subject of research over many decades. In recent years progress in our understanding of ribosome biogenesis has been rapid and is accelerating. This review discusses current understanding of how the biochemical processes of ribosome biosynthesis relate to an observable nucleolar structure. Emerging evidence is also described that points to other, unconventional roles for the nucleolus, particularly in the biogenesis of other RNA-containing cellular machinery, and in stress sensing and the control of cellular activity. Striking recent observations show that the nucleolus and its components are highly dynamic, and that the steady state structure observed by microscopical methods must be interpreted as the product of these dynamic processes. We still do not have detailed enough information to understand fully the organization and regulation of the various processes taking place in the nucleolus. However, the present power of light and electron microscopy (EM) techniques means that a description of nucleolar processes at the molecular level is now achievable, and the time is ripe for such an effort.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"255 ","pages":"177-235"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)55004-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26451770","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Plasticity of pelvic autonomic ganglia and urogenital innervation.","authors":"Janet R Keast","doi":"10.1016/S0074-7696(06)48003-7","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)48003-7","url":null,"abstract":"<p><p>Pelvic ganglia contain a mixture of sympathetic and parasympathetic neurons and provide most of the motor innervation of the urogenital organs. They show a remarkable sensitivity to androgens and estrogens, which impacts on their development into sexually dimorphic structures and provide an array of mechanisms by which plasticity of these neurons can occur during puberty and adulthood. The structure of pelvic ganglia varies widely among species, ranging from rodents, which have a pair of large ganglia, to humans, in whom pelvic ganglion neurons are distributed in a large, complex plexus. This plexus is frequently injured during pelvic surgical procedures, yet strategies for its repair have yet to be developed. Advances in this area will come from a better understanding of the effects of injury on the cellular signaling process in pelvic neurons and also the role of neurotrophic factors during development, maintenance, and repair of these axons.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"248 ","pages":"141-208"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)48003-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25863834","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}