scholarly journals Adherens Junctions and Desmosomes Coordinate Mechanics and Signaling to Orchestrate Tissue Morphogenesis and Function: An Evolutionary Perspective

2017 ◽  
Vol 10 (11) ◽  
pp. a029207 ◽  
Author(s):  
Matthias Rübsam ◽  
Joshua A. Broussard ◽  
Sara A. Wickström ◽  
Oxana Nekrasova ◽  
Kathleen J. Green ◽  
...  
2008 ◽  
Vol 4 (2) ◽  
pp. 179-182 ◽  
Author(s):  
Reuben Clements ◽  
Thor-Seng Liew ◽  
Jaap Jan Vermeulen ◽  
Menno Schilthuizen

The manner in which a gastropod shell coils has long intrigued laypersons and scientists alike. In evolutionary biology, gastropod shells are among the best-studied palaeontological and neontological objects. A gastropod shell generally exhibits logarithmic spiral growth, right-handedness and coils tightly around a single axis. Atypical shell-coiling patterns (e.g. sinistroid growth, uncoiled whorls and multiple coiling axes), however, continue to be uncovered in nature. Here, we report another coiling strategy that is not only puzzling from an evolutionary perspective, but also hitherto unknown among shelled gastropods. The terrestrial gastropod Opisthostoma vermiculum sp. nov. generates a shell with: (i) four discernable coiling axes, (ii) body whorls that thrice detach and twice reattach to preceding whorls without any reference support, and (iii) detached whorls that coil around three secondary axes in addition to their primary teleoconch axis. As the coiling strategies of individuals were found to be generally consistent throughout, this species appears to possess an unorthodox but rigorously defined set of developmental instructions. Although the evolutionary origins of O. vermiculum and its shell's functional significance can be elucidated only once fossil intermediates and live individuals are found, its bewildering morphology suggests that we still lack an understanding of relationships between form and function in certain taxonomic groups.


2011 ◽  
Vol 195 (5) ◽  
pp. 873-887 ◽  
Author(s):  
Beate K. Straub ◽  
Steffen Rickelt ◽  
Ralf Zimbelmann ◽  
Christine Grund ◽  
Caecilia Kuhn ◽  
...  

Intercellular junctions play a pivotal role in tissue development and function and also in tumorigenesis. In epithelial cells, decrease or loss of E-cadherin, the hallmark molecule of adherens junctions (AJs), and increase of N-cadherin are widely thought to promote carcinoma progression and metastasis. In this paper, we show that this “cadherin switch” hypothesis does not hold for diverse endoderm-derived cells and cells of tumors derived from them. We show that the cadherins in a major portion of AJs in these cells can be chemically cross-linked in E–N heterodimers. We also show that cells possessing E–N heterodimer AJs can form semistable hemihomotypic AJs with purely N-cadherin–based AJs of mesenchymally derived cells, including stroma cells. We conclude that these heterodimers are the major AJ constituents of several endoderm-derived tissues and tumors and that the prevailing concept of antagonistic roles of these two cadherins in developmental and tumor biology has to be reconsidered.


2019 ◽  
Vol 132 (7) ◽  
pp. jcs224063 ◽  
Author(s):  
Cordelia Rauskolb ◽  
Estelle Cervantes ◽  
Ferralita Madere ◽  
Kenneth D. Irvine

2007 ◽  
Vol 44 (2) ◽  
pp. 267-274 ◽  
Author(s):  
Hillary C Maddin ◽  
Robert R Reisz

Morphological features of the terminal phalanges of extinct tetrapods can be used to infer whether or not keratinous claws were present even though these structures are not preserved in the fossil record. Such features as dense vascularization grooves and foramina, and a general claw-like morphology, are present in some of the earliest fully terrestrial tetrapods, the Permo-Carboniferous synapsids. Early synapsids are represented by a rich fossil record that preserves the detailed anatomy of the terminal phalanges and allows for an examination of the early evolution of these structures in a well-resolved phylogenetic context. The pattern of change in the morphology of the terminal phalanges of five basal synapsids, Cotylorhynchus romeri, Varanops sp., Edaphosaurus boanerges, Haptodus garnettensis, and Dimetrodon limbatus, reveals a clear trend from a broad, flat, and spatulate morphology in the basal taxa to a tall, narrow, and curved structure. This trend in overall shape change does not reflect changes in feeding behaviour. The size and shape of the flexor tubercle appears to be a factor of size and function, rather than possessing a phylogenetically informative signal. The osteological features used to infer the presence of a keratinous sheath in the synapsids are also observed in the non-amniote taxon Diadectes absitus. This indicates that claws were not an amniote innovation and that they instead originated somewhere outside the crown group Amniota.


2018 ◽  
Author(s):  
Ekaterina Pukhlyakova ◽  
Anastasia Kirillova ◽  
Yulia Kraus ◽  
Ulrich Technau

Morphogenesis is a shape-building process during development of multicellular organisms. During this process the establishment and modulation of cell-cell contacts play an important role. Cadherins, the major cell adhesion molecules, form adherens junctions connecting epithelial cells. Numerous studies in Bilateria have shown that cadherins are associated with the regulation of cell differentiation, cell shape changes, cell migration and tissue morphogenesis. To date, the role of Cadherins in non-bilaterians is unknown. Here, we study the expression and the function of two paralogous classical cadherins, cadherin1 and cadherin3, in the diploblastic animal, the sea anemone Nematostella vectensis. We show that a cadherin switch is accompanying the formation of germ layers. Using specific antibodies, we show that both cadherins are localized to adherens junctions at apical and basal positions in ectoderm and endoderm. During gastrulation, partial EMT of endodermal cells is marked by a step-wise downregulation of cadherin3 and upregulation of cadherin1. Knockdown experiments show that both cadherins are required for maintenance of tissue integrity and tissue morphogenesis. This demonstrates that cnidarians convergently use cadherins to differentially control morphogenetic events during development.


2020 ◽  
Vol 14 ◽  
Author(s):  
Arpád Dobolyi ◽  
Szilvia Oláh ◽  
Dávid Keller ◽  
Rashmi Kumari ◽  
Emese A. Fazekas ◽  
...  

2001 ◽  
Vol 12 (11) ◽  
pp. 3465-3475 ◽  
Author(s):  
Bonnie L. Firestein ◽  
Christopher Rongo

Cellular junctions are critical for intercellular communication and for the assembly of cells into tissues. Cell junctions often consist of tight junctions, which form a permeability barrier and prevent the diffusion of lipids and proteins between cell compartments, and adherens junctions, which control the adhesion of cells and link cortical actin filaments to attachment sites on the plasma membrane. Proper tight junction formation and cell polarity require the function of membrane-associated guanylate kinases (MAGUKs) that contain the PDZ protein-protein interaction domain. In contrast, less is known about how adherens junctions are assembled. Here we describe how the PDZ-containing protein DLG-1 is required for the proper formation and function of adherens junctions in Caenorhabditis elegans. DLG-1 is a MAGUK protein that is most similar in sequence to mammalian SAP97, which is found at both synapses of the CNS, as well as at cell junctions of epithelia. DLG-1 is localized to adherens junctions, and DLG-1 localization is mediated by an amino-terminal domain shared with SAP97 but not found in other MAGUK family members. DLG-1 recruits other proteins and signaling molecules to adherens junctions, while embryos that lack DLG-1 fail to recruit the proteins AJM-1 and CPI-1 to adherens junctions. DLG-1 is required for the proper organization of the actin cytoskeleton and for the morphological elongation of embryos. In contrast to other proteins that have been observed to affect adherens junction assembly and function, DLG-1 is not required to maintain cell polarity. Our results suggest a new function for MAGUK proteins distinct from their role in cell polarity.


Sign in / Sign up

Export Citation Format

Share Document