scholarly journals A docked mutation phenocopies dumpy oblique alleles via altered vesicle trafficking

PeerJ ◽  
2021 ◽  
Vol 9 ◽  
pp. e12175
Author(s):  
Suresh Kandasamy ◽  
Kiley Couto ◽  
Justin Thackeray
Keyword(s):  
Matrix Protein ◽  
Vesicle Trafficking ◽  
Notch Pathway ◽  
Vesicle Transport ◽  
Snare Proteins ◽  
Extracellular Matrix Protein ◽  
Functional Connection ◽  
Core Proteins ◽  
Genes Encoding

The Drosophila extracellular matrix protein Dumpy (Dpy) is one of the largest proteins encoded by any animal. One class of dpy mutations produces a characteristic shortening of the wing blade known as oblique (dpyo), due to altered tension in the developing wing. We describe here the characterization of docked (doc), a gene originally named because of an allele producing a truncated wing. We show that doc corresponds to the gene model CG5484, which encodes a homolog of the yeast protein Yif1 and plays a key role in ER to Golgi vesicle transport. Genetic analysis is consistent with a similar role for Doc in vesicle trafficking: docked alleles interact not only with genes encoding the COPII core proteins sec23 and sec13, but also with the SNARE proteins synaptobrevin and syntaxin. Further, we demonstrate that the strong similarity between the doc1 and dpyo wing phenotypes reflects a functional connection between the two genes; we found that various dpy alleles are sensitive to changes in dosage of genes encoding other vesicle transport components such as sec13 and sar1. Doc’s effects on trafficking are not limited to Dpy; for example, reduced doc dosage disturbed Notch pathway signaling during wing blade and vein development. These results suggest a model in which the oblique wing phenotype in doc1 results from reduced transport of wild-type Dumpy protein; by extension, an additional implication is that the dpyo alleles can themselves be explained as hypomorphs.

scholarly journals Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21

1997 ◽  
Vol 16 (5) ◽  
pp. 289-292 ◽  
Author(s):  
Maureen R. Johnson ◽  
Douglas J. Wilkin ◽  
Hans L. Vos ◽  
Rosa Isela Ortiz De Luna ◽  
Anindya M. Dehejia ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Extracellular Matrix Protein 1 ◽  
Chromosome 1Q21

Characterization of peptidases of adult Trichuris muris

Parasitology ◽  
1994 ◽  
Vol 109 (5) ◽  
pp. 623-630 ◽  
Author(s):  
L. J. Drake ◽  
A. E. Bianco ◽  
D. A. P. Bundy ◽  
F. Ashall
Keyword(s):  
Mammalian Cells ◽  
Culture Medium ◽  
Matrix Protein ◽  
Sodium Dodecyl ◽  
Time Dependent ◽  
Extracellular Matrix Protein ◽  
Peptidase Activity ◽  
Trichuris Muris ◽  
Hydrolysis Of

Excretory/secretory (E/S) material of Trichuris muris was found to contain 2 major peptidases, Mr 85 and 105 kDa, which degrade gelatin optimally at pH 6·0 in sodium dodecyl sulphate–polyacrylamide gels. The peptidases were inactivated diisopropylfluorophosphate, leupeptin and soybean trypsin inhibitor, but were unaffected by inhibitors of aspartic-, cysteine- and metallo-peptidases, indicating that they are serine peptidases. Both enzymes were detectable within 5 h after incubation of worms in culture medium and showed a time-dependent increase in levels. Neither peptidase was detected in worm extracts, suggesting that they are activated during or following secretion from worms. Live worms degraded radio-isotope labelled extracellular matrix protein substratum derived from mammalian cells. Aminopeptidase activities capable of catalysing hydrolysis of amino acyl aminomethylcoumarin (MCA) substrates and a Z-Phe-Arg-MCA-hydrolysing cysteine peptidase activity, were detected in extracts of adult worms but not in E/S material.

scholarly journals 3317 Localization and characterization of a novel extracellular matrix protein β-IG-H3

1995 ◽  
Vol 35 ◽  
pp. S136
Author(s):  
I. Rawe ◽  
Q. Zhan ◽  
Y. Komai-Hori ◽  
R. Burrows ◽  
C.L. Kublin ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein

Characterization of Cardiac Function and Arterial Mechanics During Early Postnatal Development in Fibulin-5 Null Mice

2013 ◽  
Author(s):  
Victoria Le ◽  
Hiromi Yanagisawa ◽  
Jessica Wagenseil
Keyword(s):  
Matrix Protein ◽  
Elastic Fiber ◽  
Connective Tissue Disorder ◽  
Fiber Formation ◽  
Extracellular Matrix Protein ◽  
Elastic Fibers ◽  
Arterial Mechanics ◽  
Early Postnatal Development ◽  
Complex Process

Fibulin-5 is an extracellular matrix protein that interacts with other proteins during a complex process that results in elastic fiber formation from the elastin precursor, tropoelastin [1]. Elastic fibers are an important component of tissues requiring elasticity, including large arteries, lungs and skin. In mice lacking fibulin-5 ( Fbln5−/−), these tissues contain disorganized elastic fibers and exhibit decreased elasticity [2]. The phenotype of Fbln5−/− mice is similar to that of humans with cutis laxa, a connective tissue disorder characterized by loose skin and narrow arteries with reduced compliance.

Structural disorder and dynamics of elastinThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process.

2010 ◽  
Vol 88 (2) ◽  
pp. 239-250 ◽  
Author(s):  
Lisa D. Muiznieks ◽  
Anthony S. Weiss ◽  
Fred W. Keeley
Keyword(s):  
Matrix Protein ◽  
Peer Review Process ◽  
Structural Disorder ◽  
Extracellular Matrix Protein ◽  
Tissue Elasticity ◽  
Elastic Recoil ◽  
Conformational Disorder ◽  
Self Assembling ◽  
And Function

Elastin is a self-assembling, extracellular-matrix protein that is the major provider of tissue elasticity. Here we review structural studies of elastin from over four decades, and draw together evidence for solution flexibility and conformational disorder that is inherent in all levels of structural organization. The characterization of disorder is consistent with an entropy-driven mechanism of elastic recoil. We conclude that conformational disorder is a constitutive feature of elastin structure and function.

scholarly journals Identification and characterization of a novel extracellular matrix protein nephronectin that is associated with integrin α8β1 in the embryonic kidney

2001 ◽  
Vol 154 (2) ◽  
pp. 447-458 ◽  
Author(s):  
Ralph Brandenberger ◽  
Andrea Schmidt ◽  
James Linton ◽  
Denan Wang ◽  
Carey Backus ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Extracellular Matrix Protein ◽  
Cdna Libraries ◽  
Newborn Mouse ◽  
Metanephric Mesenchyme ◽  
Rgd Sequence ◽  
Kidney Organogenesis

The epithelial–mesenchymal interactions required for kidney organogenesis are disrupted in mice lacking the integrin α8β1. None of this integrin's known ligands, however, appears to account for this phenotype. To identify a more relevant ligand, a soluble integrin α8β1 heterodimer fused to alkaline phosphatase (AP) has been used to probe blots and cDNA libraries. In newborn mouse kidney extracts, α8β1-AP detects a novel ligand of 70–90 kD. This protein, named nephronectin, is an extracellular matrix protein with five EGF-like repeats, a mucin region containing a RGD sequence, and a COOH-terminal MAM domain. Integrin α8β1 and several additional RGD-binding integrins bind nephronectin. Nephronectin mRNA is expressed in the ureteric bud epithelium, whereas α8β1 is expressed in the metanephric mesenchyme. Nephronectin is localized in the extracellular matrix in the same distribution as the ligand detected by α8β1-AP and forms a complex with α8β1 in vivo. Thus, these results strongly suggest that nephronectin is a relevant ligand mediating α8β1 function in the kidney. Nephronectin is expressed at numerous sites outside the kidney, so it may also have wider roles in development. The approaches used here should be generally useful for characterizing the interactions of novel extracellular matrix proteins identified through genomic sequencing projects.

scholarly journals Expression and characterization of novel thrombospondin 1 type I repeat fusion proteins

2000 ◽  
Vol 346 (1) ◽  
pp. 147-153 ◽  
Author(s):  
Aziz N. QABAR ◽  
Jeff BULLOCK ◽  
Louis MATEJ ◽  
Peter POLVERINI
Keyword(s):  
Matrix Protein ◽  
Full Length ◽  
Extracellular Matrix Protein ◽  
Microvascular Endothelial Cell ◽  
Type I ◽  
Heparin Binding ◽  
Novel Structures ◽  
Trimeric Structure

Thrombospondin (TSP)1 is a trimeric extracellular matrix protein that is held together by two cysteine residues. It is one of five TSP proteins that have been described to date with almost a universal heparin binding capability (TSP5 being the exception). The existence of two conformationally distinct structures in the TSP family (trimers and pentamers) prompted us to investigate the contribution of TSP1 trimeric structure to its inhibitory role in angiogenesis. We expressed full-length recombinant human TSP1, its type I repeats, and murine TSP3 in a human embryonic kidney cell line and evaluated their effect on human dermal microvascular endothelial cell (HMVEC) proliferation and sprouting into tube-like structures in vitro. Additionally, two chimaeric molecules were constructed so that the type I repeats of TSP1 were expressed as either dimers (TSP1-Ig chimaera) or pentamers (TSP1-TSP3 chimaera). Dimeric and pentameric type I constructs are novel structures. We found that, similarly to full-length TSP1, intact trimeric type I repeats were inhibitory to HMVEC angiogenesis in vitro. However, dimeric and pentameric type I repeats of TSP1 only partially inhibited HMVEC proliferation and sprouting in vitro. TSP3, which is lacking type I repeats, had no inhibitory activity, confirming that type I repeats elicit the anti-angiogenic activity of TSP1.

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