scholarly journals Structure of human Dispatched-1 provides insights into Hedgehog ligand biogenesis

2020 ◽  
Vol 3 (8) ◽  
pp. e202000776
Author(s):  
Hongwen Chen ◽  
Yang Liu ◽  
Xiaochun Li
Keyword(s):  
Cell Surface ◽  
Extracellular Space ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Transmembrane Helices ◽  
Closed State ◽  
A Cell ◽  
Hh Signaling ◽  
Structural Homologues ◽  
Resolution Structure

Hedgehog (HH) signaling is essential for metazoan development. The HH ligand is secreted into the extracellular space by a cell surface protein named Dispatched-1 (DISP1). Here, we report the cryo-EM structure of human DISP1 protein. DISP1 contains 12 transmembrane helices (TMs) and two extracellular domains (ECDs). Its ECDs reveal an open state, in contrast to its structural homologues PTCH1 and NPC1, whose extracellular/luminal domains adopt a closed state. The low-resolution structure of the DISP1 complex with dual lipid-modified HH ligand reveals how the ECDs of DISP1 engage with HH ligand. Moreover, several cholesterol-like molecules are found in the TMs, implying a transport-like function of DISP1.

Localization and expression of msp130, a primary mesenchyme lineage-specific cell surface protein in the sea urchin embryo

Development ◽  
1987 ◽  
Vol 101 (2) ◽  
pp. 255-265 ◽  
Author(s):  
J.A. Anstrom ◽  
J.E. Chin ◽  
D.S. Leaf ◽  
A.L. Parks ◽  
R.A. Raff
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Sea Water ◽  
Surface Protein ◽  
Specific Cell ◽  
Cell Surface Protein ◽  
Sea Urchin Embryo ◽  
A Cell ◽  
Mesenchyme Cells ◽  
Primary Mesenchyme Cells

In this report, we use a monoclonal antibody (B2C2) and antibodies against a fusion protein (Leaf et al. 1987) to characterize msp130, a cell surface protein specific to the primary mesenchyme cells of the sea urchin embryo. This protein first appears on the surface of these cells upon ingression into the blastocoel. Immunoelectronmicroscopy shows that msp130 is present in the trans side of the Golgi apparatus and on the extracellular surface of primary mesenchyme cells. Four precursor proteins to msp130 are identified and we show that B2C2 recognizes only the mature form of msp130. We demonstrate that msp130 contains N-linked carbohydrate groups and that the B2C2 epitope is sensitive to endoglycosidase F digestion. Evidence that msp130 is apparently a sulphated glycoprotein is presented. The recognition of the B2C2 epitope of msp130 is disrupted when embryos are cultured in sulphate-free sea water. In addition, two-dimensional immunoblots show that msp130 is an acidic protein that becomes substantially less acidic in the absence of sulphate. We also show that two other independently derived monoclonal antibodies, IG8 (McClay et al. 1983; McClay, Matranga & Wessel, 1985) and 1223 (Carson et al. 1985), recognize msp130, and suggest this protein to be a major cell surface antigen of primary mesenchyme cells.

scholarly journals A cell surface protein controls endocrine ring gland morphogenesis and steroid production

2019 ◽  
Vol 445 (1) ◽  
pp. 16-28 ◽  
Author(s):  
Yanina-Yasmin Pesch ◽  
Ricarda Hesse ◽  
Tariq Ali ◽  
Matthias Behr
Keyword(s):  
Cell Surface ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Steroid Production ◽  
Ring Gland ◽  
A Cell ◽  
Gland Morphogenesis

scholarly journals The in silico human surfaceome

2018 ◽  
Vol 115 (46) ◽  
pp. E10988-E10997 ◽  
Author(s):  
Damaris Bausch-Fluck ◽  
Ulrich Goldmann ◽  
Sebastian Müller ◽  
Marc van Oostrum ◽  
Maik Müller ◽  
...  
Keyword(s):  
Cell Surface ◽  
In Silico ◽  
Embryonic Stem ◽  
Surface Protein ◽  
Surface Proteins ◽  
Cell Surface Protein ◽  
Cell Surface Proteins ◽  
A Cell ◽  
Visualization Tools ◽  
Protein Classes

Cell-surface proteins are of great biomedical importance, as demonstrated by the fact that 66% of approved human drugs listed in the DrugBank database target a cell-surface protein. Despite this biomedical relevance, there has been no comprehensive assessment of the human surfaceome, and only a fraction of the predicted 5,000 human transmembrane proteins have been shown to be located at the plasma membrane. To enable analysis of the human surfaceome, we developed the surfaceome predictor SURFY, based on machine learning. As a training set, we used experimentally verified high-confidence cell-surface proteins from the Cell Surface Protein Atlas (CSPA) and trained a random forest classifier on 131 features per protein and, specifically, per topological domain. SURFY was used to predict a human surfaceome of 2,886 proteins with an accuracy of 93.5%, which shows excellent overlap with known cell-surface protein classes (i.e., receptors). In deposited mRNA data, we found that between 543 and 1,100 surfaceome genes were expressed in cancer cell lines and maximally 1,700 surfaceome genes were expressed in embryonic stem cells and derivative lines. Thus, the surfaceome diversity depends on cell type and appears to be more dynamic than the nonsurface proteome. To make the predicted surfaceome readily accessible to the research community, we provide visualization tools for intuitive interrogation (wlab.ethz.ch/surfaceome). The in silico surfaceome enables the filtering of data generated by multiomics screens and supports the elucidation of the surfaceome nanoscale organization.

NYX(Nyctalopin on Chromosome X), the Gene Mutated in Congenital Stationary Night Blindness, Encodes a Cell Surface Protein

2003 ◽  
Vol 44 (10) ◽  
pp. 4184 ◽  
Author(s):  
Christina Zeitz ◽  
Harry Scherthan ◽  
Susanne Freier ◽  
Silke Feil ◽  
Vanessa Suckow ◽  
...  
Keyword(s):  
Cell Surface ◽  
Night Blindness ◽  
Surface Protein ◽  
Cell Surface Protein ◽  
Congenital Stationary Night Blindness ◽  
Chromosome X ◽  
A Cell

Developmental expression of a cell-surface protein involved in calcium uptake and skeleton formation in sea urchin embryos

1987 ◽  
Vol 122 (2) ◽  
pp. 320-331 ◽  
Author(s):  
Mary C. Farach ◽  
Maria Valdizan ◽  
Helen R. Park ◽  
Glenn L. Decker ◽  
William J. Lennarz
Keyword(s):  
Cell Surface ◽  
Sea Urchin ◽  
Calcium Uptake ◽  
Surface Protein ◽  
Developmental Expression ◽  
Cell Surface Protein ◽  
Sea Urchin Embryos ◽  
A Cell ◽  
Skeleton Formation
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