Extracellular chloride signals collagen IV network assembly during basement membrane formation

Cummings, Christopher F.; Pedchenko, Vadim; Brown, Kyle L.; Colon, Selene; Rafi, Mohamed; Jones-Paris, Celestial R.; Pokydeshava, Elena; Liu, Min; Pastor-Pareja, José Carlos; Stothers, Cody L.; Ero-Tolliver, Isi A.; McCall, A. Scott; Vanacore, Roberto M.; Bhave, Gautam; Santoro, Samuel A.; Blackwell, Timothy S.; Zent, Roy; Pozzi, Ambra; Hudson, Billy G.

doi:10.1083/jcb.201510065

Cited by 59 publications

(105 citation statements)

References 70 publications

(101 reference statements)

Supporting

Mentioning

101

Contrasting

Order By: Relevance

“…Protomers form through the self‐assembly of three collagen IV α‐chains. NC1 domains nucleate protomer assembly through a mechanism that regulates chain selection and triggers winding of the triple helix toward the N‐termini (Fig. ).…”

Section: Overview Of Scaffold Assemblymentioning

confidence: 99%

“…Oligomerization at the NC1 domain is driven through ionic Cl − driven activation of a molecular switch within individual protomers enabling binding of a neighboring protomer (Fig. ) . The 7S domains assemble into dodecameric structures (e.g., heterotrimeric 7S domains from a complex of four independent protomers).…”

Section: Overview Of Scaffold Assemblymentioning

confidence: 99%

“…NC1 trimerization is a seminal event in protomer assembly that governs chain selection, registration, and stoichiometry . Although there are six collagen IV chains (α1–6) allowing for numerous potential trimeric protomers, the chain composition of assembled protomers is restricted to only three combinations: α112, α345, and α556.…”

Section: Stages Of Scaffold Assemblymentioning

confidence: 99%

See 2 more Smart Citations

Building collagen IV smart scaffolds on the outside of cells

Brown

Cummings²,

Vanacore

et al. 2017

Protein Science

Self Cite

View full text Add to dashboard Cite

Collagen IV scaffolds assemble through an intricate pathway that begins intracellularly and is completed extracellularly. Multiple intracellular enzymes act in concert to assemble collagen IV protomers, the building blocks of collagen IV scaffolds. After being secreted from cells, protomers are activated to initiate oligomerization, forming insoluble networks that are structurally reinforced with covalent crosslinks. Within these networks, embedded binding sites along the length of the protomer lead to the "decoration" of collagen IV triple helix with numerous functional molecules. We refer to these networks as "smart" scaffolds, which as a component of the basement membrane enable the development and function of multicellular tissues in all animal phyla. In this review, we present key molecular mechanisms that drive the assembly of collagen IV smart scaffolds.

show abstract

Section: Overview Of Scaffold Assemblymentioning

confidence: 99%

Section: Overview Of Scaffold Assemblymentioning

confidence: 99%

Section: Stages Of Scaffold Assemblymentioning

confidence: 99%

See 1 more Smart Citation

Building collagen IV smart scaffolds on the outside of cells

Brown

Cummings²,

Vanacore

et al. 2017

Protein Science

Self Cite

View full text Add to dashboard Cite

show abstract

“…The lack of these reinforcements led to early developmental disorders and dysfunction in several tissues and organisms [26–30]. However, observations of the dynamic distribution of peroxidasin in BMs is limited to development of C. elegan tissues [31] and cell lines [32], and has been implied in embryonic mouse tissues [29]. Extracellular GPBP was discovered through its binding to kidney BM [33] and has since been shown to bind major BM components laminin and collagen IV [34,35].…”

Section: Introductionmentioning

confidence: 99%

Embryo implantation triggers dynamic spatiotemporal expression of the basement membrane toolkit during uterine reprogramming

et al. 2017

Self Cite

View full text Add to dashboard Cite

Basement membranes (BMs) are specialized extracellular scaffolds that influence behaviors of cells in epithelial, endothelial, muscle, nervous, and fat tissues. Throughout development and in response to injury or disease, BMs are fine-tuned with specific protein compositions, ultrastructure, and localization. These features are modulated through implements of the BM toolkit that is comprised of collagen IV, laminin, perlecan, and nidogen. Two additional proteins, peroxidasin and Goodpasture antigen-binding protein (GPBP), have recently emerged as potential members of the toolkit. In the present study, we sought to determine whether peroxidasin and GPBP undergo dynamic regulation in the assembly of uterine tissue BMs in early pregnancy as a tractable model for dynamic adult BMs. We explored these proteins in the context of collagen IV and laminin that are known to extensively change for decidualization. Electron microscopic analyses revealed: 1) a smooth continuous layer of BM in between the epithelial and stromal layers of the preimplantation endometrium; and 2) interrupted, uneven, and progressively thickened BM within the pericellular space of the postimplantation decidua. Quantification of mRNA levels by qPCR showed changes in expression levels that were complemented by immunofluorescence localization of peroxidasin, GPBP, collagen IV, and laminin. Novel BM-associated and subcellular spatiotemporal localization patterns of the four components suggest both collective pericellular functions and distinct functions in the uterus during reprogramming for embryo implantation.

show abstract

“…How the various components of basement membranes are assembled into an organized network that can regulate the behavior of overlying cells remains unclear (1), but now describe how extracellular chloride ions induce the higher order assembly of collagen IV molecules outside the cell (2). …”

mentioning

confidence: 99%