BioarchitecturePub Date : 2016-01-01Epub Date: 2016-10-14DOI: 10.1080/19490992.2016.1229729
Melissa L Knothe Tate, Peter W Gunning, Vittorio Sansalone
{"title":"Emergence of Form from Function - Mechanical Engineering Approaches to Probe the Role of Stem Cell Mechanoadaptation in Sealing Cell Fate.","authors":"Melissa L Knothe Tate, Peter W Gunning, Vittorio Sansalone","doi":"10.1080/19490992.2016.1229729","DOIUrl":"https://doi.org/10.1080/19490992.2016.1229729","url":null,"abstract":"<p><p>Stem cell \"mechanomics\" refers to the effect of mechanical cues on stem cell and matrix biology, where cell shape and fate are intrinsic manifestations of form and function. Before specialization, the stem cell itself serves as a sensor and actuator; its structure emerges from its local mechanical milieu as the cell adapts over time. Coupling of novel spatiotemporal imaging and computational methods allows for linking of the energy of adaptation to the structure, biology and mechanical function of the cell. Cutting edge imaging methods enable probing of mechanisms by which stem cells' emergent anisotropic architecture and fate commitment occurs. A novel cell-scale model provides a mechanistic framework to describe stem cell growth and remodeling through mechanical feedback; making use of a generalized virtual power principle, the model accounts for the rate of doing work or the rate of using energy to effect the work. This coupled approach provides a basis to elucidate mechanisms underlying the stem cell's innate capacity to adapt to mechanical stimuli as well as the role of mechanoadaptation in lineage commitment. An understanding of stem cell mechanoadaptation is key to deciphering lineage commitment, during prenatal development, postnatal wound healing, and engineering of tissues.</p>","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"6 5","pages":"85-103"},"PeriodicalIF":0.0,"publicationDate":"2016-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19490992.2016.1229729","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39975353","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioarchitecturePub Date : 2015-12-02DOI: 10.1080/19490992.2015.1127466
D. D. Richardson, M. Fernandez-Borja
{"title":"Leukocyte adhesion and polarization: Role of glycosylphosphatidylinositol-anchored proteins","authors":"D. D. Richardson, M. Fernandez-Borja","doi":"10.1080/19490992.2015.1127466","DOIUrl":"https://doi.org/10.1080/19490992.2015.1127466","url":null,"abstract":"ABSTRACT Leukocyte traffic out of the blood stream is crucial for an adequate immune response. Leukocyte extravasation is critically dependent on the binding of leukocyte integrins to their endothelial counterreceptors. This interaction enables the firm adhesion of leukocytes to the luminal side of the vascular wall and allows for leukocyte polarization, crawling and diapedesis. Leukocyte adhesion, polarization and migration requires the orchestrated regulation of integrin adhesion/de-adhesion dynamics and actin cytoskeleton rearrangements. Adhesion strength depends on conformational changes of integrin molecules (affinity) as well as the number of integrin molecules engaged at adhesion sites (valency). These two processes can be independently regulated and several molecules modulate either one or both processes. Cholesterol-rich membrane domains (lipid rafts) participate in integrin regulation and play an important role in leukocyte adhesion, polarization and motility. In particular, lipid raft-resident glycosyl-phosphatidyl-inositol-anchored proteins (GPI-APs) have been reported to regulate leukocyte adhesion, polarization and motility in both integrin-dependent and independent manners. Here, we present our recent discovery concerning the novel role of the GPI-AP prion protein (PrP) in the regulation of β1 integrin-mediated monocyte adhesion, migration and shape polarization in the context of existing literature on GPI-AP-dependent regulation of integrins.","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"2 1","pages":"61 - 69"},"PeriodicalIF":0.0,"publicationDate":"2015-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76720839","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}
BioarchitecturePub Date : 2015-12-02DOI: 10.1080/19490992.2015.1128604
Y. Senju, S. Suetsugu
{"title":"Possible regulation of caveolar endocytosis and flattening by phosphorylation of F-BAR domain protein PACSIN2/Syndapin II","authors":"Y. Senju, S. Suetsugu","doi":"10.1080/19490992.2015.1128604","DOIUrl":"https://doi.org/10.1080/19490992.2015.1128604","url":null,"abstract":"ABSTRACT. Caveolae are flask-shaped invaginations of the plasma membrane. The BAR domain proteins form crescent-shaped dimers, and their oligomeric filaments are considered to form spirals at the necks of invaginations, such as clathrin-coated pits and caveolae. PACSIN2/Syndapin II is one of the BAR domain-containing proteins, and is localized at the necks of caveolae. PACSIN2 is thought to function in the scission and stabilization of caveolae, through binding to dynamin-2 and EHD2, respectively. These two functions are considered to be switched by PACSIN2 phosphorylation by protein kinase C (PKC) upon hypotonic stress and sheer stress. The phosphorylation decreases the membrane binding affinity of PACSIN2, leading to its removal from caveolae. The removal of the putative oligomeric spiral of PACSIN2 from caveolar membrane invaginations could lead to the deformation of caveolae. Indeed, PACSIN2 removal from caveolae is accompanied by the recruitment of dynamin-2, suggesting that the removal provides space for the function of dynamin-2. Otherwise, the removal of PACSIN2 decreases the stability of caveolae, which could result in the flattening of caveolae. In contrast, an increase in the amount of EHD2 restored caveolar stability. Therefore, PACSIN2 at caveolae stabilizes caveolae, but its removal by phosphorylation could induce both caveolar endocytosis and flattening.","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"149 1","pages":"70 - 77"},"PeriodicalIF":0.0,"publicationDate":"2015-12-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82838170","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}
BioarchitecturePub Date : 2015-10-03DOI: 10.1080/19490992.2015.1106061
Shuoshuo Wang, T. Volk
{"title":"Composite biopolymer scaffolds shape muscle nucleus: Insights and perspectives from Drosophila","authors":"Shuoshuo Wang, T. Volk","doi":"10.1080/19490992.2015.1106061","DOIUrl":"https://doi.org/10.1080/19490992.2015.1106061","url":null,"abstract":"Contractile muscle fibers produce enormous intrinsic forces during contraction/relaxation waves. These forces are directly applied to their cytoplasmic organelles including mitochondria, sarcoplasmic reticulum, and multiple nuclei. Data from our analysis of Drosophila larval somatic muscle fibers suggest that an intricate network of organized microtubules (MT) intermingled with Spectrin-Repeat-Containing Proteins (SRCPs) are major structural elements that protect muscle organelles and maintain their structure and position during muscle contraction. Whereas the perinuclear MT network provides structural rigidity to the myonucleus, the SRCPs Nesprin and Spectraplakin form semiflexible filamentous biopolymer networks, providing nuclei with the elasticity required to resist the contractile cytoplasmic forces produced by the muscle. Spectrin repeats are domains found in numerous structural proteins, which are able to unfold under tension and are subject to mechanical stresses in the cell. This unique composite scaffold combines rigidity and resilience in order to neutralize the oscillating cellular forces occurring during muscle contraction/relaxation waves and thereby protect myonuclei. We suggest that the elastic properties of SRCPs are critical for nuclear protection and proper function in muscle fibers.","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"44 1","pages":"35 - 43"},"PeriodicalIF":0.0,"publicationDate":"2015-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74348771","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}
BioarchitecturePub Date : 2015-10-03DOI: 10.1080/19490992.2015.1118194
Iryna Leshchyns’ka, V. Sytnyk
{"title":"Intracellular transport and cell surface delivery of the neural cell adhesion molecule (NCAM)","authors":"Iryna Leshchyns’ka, V. Sytnyk","doi":"10.1080/19490992.2015.1118194","DOIUrl":"https://doi.org/10.1080/19490992.2015.1118194","url":null,"abstract":"ABSTRACT The neural cell adhesion molecule (NCAM) regulates differentiation and functioning of neurons by accumulating at the cell surface where it mediates the interactions of neurons with the extracellular environment. NCAM also induces a number of intracellular signaling cascades, which coordinate interactions at the cell surface with intracellular processes including changes in gene expression, transport and cytoskeleton remodeling. Since NCAM functions at the cell surface, its transport and delivery to the cell surface play a critical role. Here, we review recent advances in our understanding of the molecular mechanisms of the intracellular transport and cell surface delivery of NCAM. We also discuss the data suggesting a possibility of cross talk between activation of NCAM at the cell surface and the intracellular transport and cell surface delivery of NCAM.","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"1 1","pages":"54 - 60"},"PeriodicalIF":0.0,"publicationDate":"2015-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"89890286","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}
BioarchitecturePub Date : 2015-10-03DOI: 10.1080/19490992.2015.1102826
George Galea, J. Simpson
{"title":"High-content analysis of Rab protein function at the ER-Golgi interface","authors":"George Galea, J. Simpson","doi":"10.1080/19490992.2015.1102826","DOIUrl":"https://doi.org/10.1080/19490992.2015.1102826","url":null,"abstract":"ABSTRACT The Rab family of small GTPases play fundamental roles in the regulation of trafficking pathways between intracellular membranes in eukaryotic cells. In this short commentary we highlight a recent high-content screening study that investigates the roles of Rab proteins in retrograde trafficking from the Golgi complex to the endoplasmic reticulum, and we discuss how the findings of this work and other literature might influence our thoughts on how the architecture of the Golgi complex is regulated.","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"57 1","pages":"44 - 53"},"PeriodicalIF":0.0,"publicationDate":"2015-10-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"82651905","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}
BioarchitecturePub Date : 2015-08-03DOI: 10.1080/19490992.2015.1080891
E. Welch, F. Pelegri
{"title":"Cortical depth and differential transport of vegetally localized dorsal and germ line determinants in the zebrafish embryo","authors":"E. Welch, F. Pelegri","doi":"10.1080/19490992.2015.1080891","DOIUrl":"https://doi.org/10.1080/19490992.2015.1080891","url":null,"abstract":"ABSTRACT In zebrafish embryos, factors involved in both axis induction and primordial germ cell (PGC) development are localized to the vegetal pole of the egg. However, upon egg activation axis induction factors experience an asymmetric off-center shift whereas PGC factors undergo symmetric animally-directed movement. We examined the spatial relationship between the proposed dorsal genes wnt8a and grip2a and the PGC factor dazl at the vegetal cortex. We find that RNAs for these genes localize to different cortical depths, with the RNA for the PGC factor dazl at a deeper cortical level than those for axis-inducing factors. In addition, and in contrast to the role of microtubules in the long-range transport of dorsal determinants, we find that germ line determinant transport depends on the actin cytoskeleton. Our results support a model in which vegetal cortex differential RNA transport behavior is facilitated by RNA localization along cortical depth and differential coupling to cortical transport.","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"19 1","pages":"13 - 26"},"PeriodicalIF":0.0,"publicationDate":"2015-08-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"85117386","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}
BioarchitecturePub Date : 2015-01-01Epub Date: 2015-10-02DOI: 10.1080/19490992.2015.1090669
Shivangi Agarwal, Dileep Varma
{"title":"How the SAC gets the axe: Integrating kinetochore microtubule attachments with spindle assembly checkpoint signaling.","authors":"Shivangi Agarwal, Dileep Varma","doi":"10.1080/19490992.2015.1090669","DOIUrl":"https://doi.org/10.1080/19490992.2015.1090669","url":null,"abstract":"<p><p>Mitosis entails the bona fide segregation of duplicated chromosomes. This process is accomplished by the attachment of kinetochores on chromosomes to microtubules (MTs) of the mitotic spindle. Once the appropriate attachment is achieved, the spindle assembly checkpoint (SAC) that delays the premature onset of anaphase needs to be silenced for the cell to proceed to anaphase and cytokinesis. Therefore, while it is imperative to preserve the SAC when kinetochores are unattached, it is of paramount importance that SAC components are removed post kinetochore microtubule (kMT) attachment. Precise knowledge of how kMT attachments trigger the removal of SAC components from kinetochores or how the checkpoint proteins feedback in to the attachment machinery remains elusive. This review aims to describe the recent advances that provide an insight into the interplay of molecular events that coordinate and regulate the SAC activity in response to kMT attachment during cell division.</p>","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"5 1-2","pages":"1-12"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19490992.2015.1090669","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34056102","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioarchitecturePub Date : 2014-03-01Epub Date: 2014-05-21DOI: 10.4161/bioa.29070
Leif Dehmelt
{"title":"Cytoskeletal self-organization in neuromorphogenesis.","authors":"Leif Dehmelt","doi":"10.4161/bioa.29070","DOIUrl":"https://doi.org/10.4161/bioa.29070","url":null,"abstract":"<p><p>Self-organization of dynamic microtubules via interactions with associated motors plays a critical role in spindle formation. The microtubule-based mechanisms underlying other aspects of cellular morphogenesis, such as the formation and development of protrusions from neuronal cells is less well understood. In a recent study, we investigated the molecular mechanism that underlies the massive reorganization of microtubules induced in non-neuronal cells by expression of the neuronal microtubule stabilizer MAP2c. In that study we directly observed cortical dynein complexes and how they affect the dynamic behavior of motile microtubules in living cells. We found that stationary dynein complexes transiently associate with motile microtubules near the cell cortex and that their rapid turnover facilitates efficient microtubule transport. Here, we discuss our findings in the larger context of cellular morphogenesis with specific focus on self-organizing principles from which cellular shape patterns such as the thin protrusions of neurons can emerge. </p>","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"4 2","pages":"75-80"},"PeriodicalIF":0.0,"publicationDate":"2014-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bioa.29070","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32356141","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
BioarchitecturePub Date : 2014-03-01Epub Date: 2014-04-07DOI: 10.4161/bioa.28516
Volney L Sheen
{"title":"Filamin A and Big2: a shared endocytic pathway.","authors":"Volney L Sheen","doi":"10.4161/bioa.28516","DOIUrl":"https://doi.org/10.4161/bioa.28516","url":null,"abstract":"<p><p>Neural proliferation, migration and differentiation require reorganization of the actin cytoskeleton and regulation of vesicle trafficking to provide stability in maintaining cell adhesions, allow for changes in cell shape, and establishing cell polarity. Human disorders involving the actin-binding Filamin A (FLNA) and vesicle trafficking Brefeldin-associated guanine exchange factor 2 (BIG2 is encoded by the ARFGEF2 gene) proteins are implicated in these various developmental processes, resulting in a malformation of cortical development called periventricular heterotopia (nodules along the ventricular lining) and microcephaly (small brain). Here we discuss several recent reports from our laboratory that demonstrate a shared role for both proteins in actin-associated vesicle trafficking, which is required to maintain the expression and stability of cell adhesion and cell cycle associated molecules during cortical development. While changes in FLNA and BIG2 have first been linked to disorders involving the central nervous system, increasing reports suggest they are associated with aberrant development of various other organ systems in the body. These studies suggest that vesicle trafficking defects in FLN-GEF dependent pathways may contribute to a much broader phenotype than previously realized. </p>","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"4 2","pages":"53-7"},"PeriodicalIF":0.0,"publicationDate":"2014-03-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bioa.28516","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32242457","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}