{"title":"The polymeric immunoglobulin receptor","authors":"Keith E. Mostov","doi":"10.1002/9780470015902.A0024237","DOIUrl":"https://doi.org/10.1002/9780470015902.A0024237","url":null,"abstract":"As a model system to study protein traffic in epithelial cells we have used the polymeric immunoglobulin receptor. This receptor travels first to the basolateral surface where it can bind polymeric IgA or IgM. The receptor is then endocytosed and delivered to endosomes. The receptor is sorted into transcytotic vesicles which are exocytosed at the apical surface. The 103 amino acid cytoplasmic domain of the receptor contains several sorting signals. The 17 residues closest to the membrane are an autonomous signal for basolateral sorting. For endocytosis there are two signals, both of which contain tyrosines. Finally, transcytosis is signaled by serine phosphorylation.","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"2 1","pages":"411-418"},"PeriodicalIF":0.0,"publicationDate":"2013-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"51133434","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":"Mechanisms of mitotic spindle assembly and function.","authors":"Claire E Walczak, Rebecca Heald","doi":"10.1016/S0074-7696(07)65003-7","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65003-7","url":null,"abstract":"<p><p>The mitotic spindle is the macromolecular machine that segregates chromosomes to two daughter cells during mitosis. The major structural elements of the spindle are microtubule polymers, whose intrinsic polarity and dynamic properties are critical for bipolar spindle organization and function. In most cell types, spindle microtubule nucleation occurs primarily at two centrosomes, which define the spindle poles, but microtubules can also be generated by the chromosomes and within the spindle itself. Many associated factors help organize the spindle, including molecular motors and regulators of microtubule dynamics. The past decade has provided a wealth of information on the molecular players that are critical for spindle assembly as well as a high-resolution view of the intricate movements and dynamics of the spindle microtubules and the chromosomes. In this chapter we provide a historical account of the key observations leading to current models of spindle assembly, as well as an up-to-date status report on this exciting field.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"111-58"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65003-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266871","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 the striated muscle dystrophin-glycoprotein complex.","authors":"James M Ervasti, Kevin J Sonnemann","doi":"10.1016/S0074-7696(07)65005-0","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65005-0","url":null,"abstract":"<p><p>Since its first description in 1990, the dystrophin-glycoprotein complex has emerged as a critical nexus for human muscular dystrophies arising from defects in a variety of distinct genes. Studies in mammals widely support a primary role for the dystrophin-glycoprotein complex in mechanical stabilization of the plasma membrane in striated muscle and provide hints for secondary functions in organizing molecules involved in cellular signaling. Studies in model organisms confirm the importance of the dystrophin-glycoprotein complex for muscle cell viability and have provided new leads toward a full understanding of its secondary roles in muscle biology.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"191-225"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65005-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266873","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":"Cross-talk among integrin, cadherin, and growth factor receptor: roles of nectin and nectin-like molecule.","authors":"Hisakazu Ogita, Yoshimi Takai","doi":"10.1016/S0074-7696(07)65001-3","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65001-3","url":null,"abstract":"<p><p>Integrin, cadherin, and growth factor receptor are key molecules for fundamental cellular functions including cell movement, proliferation, differentiation, adhesion, and survival. These cell surface molecules cross-talk with each other in the regulation of such cellular functions. Nectin and nectin-like molecule (Necl) have been identified as cell adhesion molecules that belong to the immunoglobulin superfamily. Nectin and Necl play important roles in the integration of integrin, cadherin, and growth factor receptor at the cell-cell adhesion sites of contacting cells and at the leading edges of moving cells, and thus are also involved in the fundamental cellular functions together with integrin, cadherin, and growth factor receptor. This chapter describes how newly identified cell adhesion molecules, nectin and Necl, modulate the cross-talk among integrin, cadherin, and growth factor receptor and how these integrated molecules act in the regulation of fundamental cellular functions.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"1-54"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65001-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266331","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}
Ian P Y Lam, Francis K Y Siu, Jessica Y S Chu, Billy K C Chow
{"title":"Multiple actions of secretin in the human body.","authors":"Ian P Y Lam, Francis K Y Siu, Jessica Y S Chu, Billy K C Chow","doi":"10.1016/S0074-7696(07)65004-9","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65004-9","url":null,"abstract":"<p><p>The discovery of secretin initiated the field of endocrinology. Over the past century, multiple gastrointestinal functions of secretin have been extensively studied, and it was discovered that the principal function of this peptide in the gastrointestinal system is to facilitate digestion and to provide protection. In view of the late identification of secretin and the secretin receptor in various tissues, including the central nervous system, the pleiotropic functions of secretin have more recently been an area of intense focus. Secretin is a classical hormone, and recent studies clearly showed secretin's involvement in neural and neuroendocrine pathways, although the neuroactivity and neural regulation of its release are yet to be elucidated. This chapter reviews our current understanding of the pleiotropic actions of secretin with a special focus on the hormonal and neural interdependent pathways that mediate these actions.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"159-90"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65004-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266872","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":"Providing unique insight into cell biology via atomic force microscopy.","authors":"Victor Shahin, Nelson P Barrera","doi":"10.1016/S0074-7696(07)65006-2","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65006-2","url":null,"abstract":"<p><p>The invention of atomic force microscopy (AFM) some two decades ago opened up new realms for our perception of cell biology. AFM produces three-dimensional images of biological surfaces at atomic resolution in physiologically relevant environments. Beyond this one-of-a-kind capability, AFM can be applied to cell biology for a variety of investigations, such as to recognize single molecules at work and study their function and structure. This admirable technique is also being widely applied to measure forces, study characteristic surface properties such as adhesion, and detect mechanical responses, for example, volume and elasticity changes of cells to various physiological and pathophysiological stimuli. In more recent years, AFM has become the most rapidly developing imaging technique. In this chapter, the AFM capabilities and the usefulness of its broad application to cell biology are highlighted, with the emphasis on structural and functional investigations into a number of biological samples focusing on cells, membranes, and single molecules.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"227-52"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65006-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266874","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":"Characteristics of oxysterol binding proteins.","authors":"Daoguang Yan, Vesa M Olkkonen","doi":"10.1016/S0074-7696(07)65007-4","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65007-4","url":null,"abstract":"<p><p>Protein families characterized by a ligand binding domain related to that of oxysterol binding protein (OSBP) have been identified in eukaryotic species from yeast to humans. These proteins, designated OSBP-related (ORP) or OSBP-like (OSBPL) proteins, have been implicated in various cellular functions. However, the detailed mechanisms of their action have remained elusive. Data from our and other laboratories suggest that binding of sterol ligands may be a unifying theme. Work with Saccharomyces cerevisiae ORPs suggests a function of these proteins in the nonvesicular intracellular transport of sterols, in secretory vesicle transport from the Golgi complex, and in the establishment of cell polarity. Mammals have more ORP genes, and differential splicing substantially increases the complexity of the encoded protein family. Functional studies on mammalian ORPs point in different directions: integration of sterol and sphingomyelin metabolism, sterol transport, regulation of neutral lipid metabolism, control of the microtubule-dependent motility of endosomes/lysosomes, and regulation of signaling cascades. We envision that during evolution, the functions of ORPs have diverged from an ancestral one in sterol transport, to meet the increasing demand of the regulatory potential in multicellular organisms. Our working hypothesis is that mammalian ORPs mainly act as sterol sensors that relay information to a spectrum of different cellular processes.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"253-85"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65007-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266875","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}
A V Revishchin, L I Korochkin, V E Okhotin, G V Pavlova
{"title":"Neural stem cells in the mammalian brain.","authors":"A V Revishchin, L I Korochkin, V E Okhotin, G V Pavlova","doi":"10.1016/S0074-7696(07)65002-5","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)65002-5","url":null,"abstract":"<p><p>New fundamental results on stem cell biology have been obtained in the past 15 years. These results allow us to reinterpret the functioning of the cerebral tissue in health and disease. Proliferating stem cells have been found in the adult brain, which can be involved in postinjury repair and can replace dead cells under specific conditions. Numerous genomic mechanisms controlling stem cell proliferation and differentiation have been identified. The involvement of stem cells in the genesis of malignant tumors has been demonstrated. Neural stem cell tropism toward tumors has been shown. These findings suggest new lines of research on brain functioning and development. Stem cells can be used to develop radically new treatments of neurodegenerative and cancer diseases of the brain.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"265 ","pages":"55-109"},"PeriodicalIF":0.0,"publicationDate":"2008-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)65002-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"27266332","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":"Auxin-mediated lateral root formation in higher plants.","authors":"Hidehiro Fukaki, Yoko Okushima, Masao Tasaka","doi":"10.1016/S0074-7696(07)56004-3","DOIUrl":"https://doi.org/10.1016/S0074-7696(07)56004-3","url":null,"abstract":"<p><p>Lateral root (LR) formation is an important organogenetic process that contributes to the establishment of root architecture in higher plants. In the angiosperms, LRs are initiated from the pericycle, an inner cell layer of the parent roots. Auxin is a key plant hormone that promotes LR formation, but the molecular mechanisms of auxin-mediated LR formation remain unknown. Molecular genetic studies using Arabidopsis mutants have revealed that the auxin transport system with a balance of influx and efflux is important for LR initiation and subsequent LR primordium development. In addition, normal auxin signaling mediated by two families of transcriptional regulators, Aux/IAAs and ARFs, is necessary for LR formation. This article is an update on the mechanisms of auxin-mediated LR formation in higher plants, particularly in Arabidopsis.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"256 ","pages":"111-37"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(07)56004-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26504692","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":"Flagellar length control in chlamydomonas--paradigm for organelle size regulation.","authors":"Kimberly A Wemmer, Wallace F Marshall","doi":"10.1016/S0074-7696(06)60004-1","DOIUrl":"https://doi.org/10.1016/S0074-7696(06)60004-1","url":null,"abstract":"<p><p>A fundamental unsolved question in cell biology is how the cell controls the size of its organelles. Cilia and flagella are an ideal test case to study the mechanism of organelle size control, because their size is easily measured and can be represented by a single number-length. Moreover, the involvement of cilia in many developmental and physiological processes suggests an understanding of their size control system is critical for understanding ciliary diseases, many of which (e.g., autosomal recessive polycystic kidney disease) are known to involve abnormally short cilia. The flagella of the model organism Chlamydomonas reinhardtii provide the best genetic and cell-biological system to study length control of cilia. Studies in this organism using genetics, biochemistry, imaging, and mathematical modeling have revealed many genes involved in length control of cilia and flagella, and have suggested several testable models for length regulation.</p>","PeriodicalId":54930,"journal":{"name":"International Review of Cytology-A Survey of Cell Biology","volume":"260 ","pages":"175-212"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0074-7696(06)60004-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26706179","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}