Inter-adipocyte Adhesion and Signaling by Collagen IV Intercellular Concentrations in Drosophila

Dai, Jianli; Ma, Mingfang; Feng, Zhi Jing; Pastor-Pareja, José Carlos

doi:10.1016/j.cub.2017.08.002

Cited by 38 publications

(42 citation statements)

References 52 publications

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“…In contrast to the accumulation of Col(IV) in SPARC protein-null larvae, overexpression of SPARC in a wild-type background resulted in a near absence of Col(IV) within the fat body. Consistent with a previous study (Dai et al, 2017), this loss of Col(IV) in the BM surrounding the fat body was observed in 3 rd instar larvae. In addition, individual adipocytes within the fat body were rounded and partially dissociated, as shown by SEM (Fig.…”

Section: Resultssupporting

confidence: 92%

Collagen-binding byDrosophilaSPARC is essential for survival and for collagen IV distribution and assembly into basement membranes

Duncan

Delage

Chioran

et al. 2019

Preprint

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Section: Resultssupporting

confidence: 92%

Collagen-binding byDrosophilaSPARC is essential for survival and for collagen IV distribution and assembly into basement membranes

Duncan

Delage

Chioran

et al. 2019

Preprint

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“…When the MTOC is disrupted, secretion of collagen and other BM proteins are impaired as a consequence of plasma membrane overgrowth due to an imbalance in membrane trafficking from blocked retrograde endosomal trafficking. This is consistent with electron microscopic analysis of fat body plasma membranes following endocytic block, where the plasma membrane becomes highly convoluted and traps secreted BM proteins and prevents them from exiting the fat body surface (Dai et al, 2017). The ncMTOC is essential to provide trafficking conduits for endocytic vesicles to restrict plasma membrane growth, and a failure to restrict membrane growth traps BM proteins in the convoluted and thickened membrane and blocks their release ( Fig 38C).…”

Section: The Fat Body Ncmtoc Controls Nuclear Positioning and Plasma supporting

confidence: 84%

“…(Viking (vkg)) ( Figure 29A). A small fraction of secreted collagen IV is incorporated into fat body cell junctions as collagen IV intercellular concentrations (CIVICs) (Dai et al, 2017), but the majority is secreted, transported via the hemolymph, and deposited along with other BM components, like Perlecan (Trol), LanB1 and Nidogen (Ndg) at destination organs like imaginal discs and the brain ( Figure 29A) (Pastor-Pareja and Xu, 2011).…”

Section: The Fat Body Ncmtoc Is Essential For Basement Membrane (Bm) mentioning

confidence: 99%

A perinuclear microtubule-organizing center controls nuclear positioning and basement membrane secretion

Zheng¹,

Buchwalter²,

Zheng³

et al. 2019

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Non-centrosomal microtubule-organizing centers (ncMTOCs) have a variety of roles presumed to serve the diverse functions of the range of cell types in which they are found. ncMTOCs are diverse in their composition, subcellular localization, and function. Here we report a novel perinuclear MTOC in Drosophila fat body cells that is anchored by Msp300/Nesprin at the cytoplasmic surface of the nucleus. Msp300 recruits the MT minus-end protein Patronin/CAMSAP, which functions redundantly with Ninein to further recruit the MT polymerase Msps/XMAP215 to assemble noncentrosomal MTs and does so independently of the widespread MT nucleation factor g-tubulin.Functionally, the fat body ncMTOC and the radial MT arrays it organizes is essential for nuclear positioning and for secretion of basement membrane components via retrograde dynein-dependent endosomal trafficking that restricts plasma membrane growth. Together, this study identifies a perinuclear ncMTOC with unique architecture and MT regulation properties that serves vital functions. Highlights• A novel perinuclear MTOC in differentiated fat body cells • The predominant nucleator, g-tubulin, is not required at the fat body ncMTOC • Msp300/Nesprin organizes the ncMTOC at the nuclear surface by recruiting Patronin/CAMSAP and the spectraplakin Shot • Patronin cooperates with Ninein to control MT assembly at the fat body ncMTOC by recruiting Msps • Msps, a MT polymerase, is essential for radial MT elongation from the fat body ncMTOC • Patronin and Msps associate • The ncMTOC and radial MTs, but not actin, control nuclear positioning in the fat body • The fat body MTOC controls retrograde endocytic trafficking to regulate plasma membrane growth and secretion of basement membrane proteins Here we report the discovery of an ncMTOC that is assembled on the surface of nuclei in Drosophila larval fat body cells, a differentiated cell type that has critical secretory functions and serves the metabolic needs of the organism. Assembly of this perinuclear ncMTOC requires the Msp300/Nesprin (nuclear envelope spectrin repeat protein) as a primary organizer/anchor. Msp300 recruits Patronin, which functions redundantly with Ninein for MT assembly at the ncMTOC. Patronin and Ninein cooperate to recruit Msps, which is essential for the elongation of MTs from the fat body ncMTOC. Recruitment of Msps and MT assembly at the ncMTOC are independent of g-tubulin. Functionally, this ncMTOC is necessary for: 1) the regulation of nuclear positioning, 2) controlling plasma membrane growth by facilitating dynein/Rab5-mediated retrograde endosomal trafficking of excess plasma membrane, and 3) the secretion of collagen IV and other basement membrane (BM) proteins. Together, this study identifies a unique perinuclear ncMTOC with novel MT assembly mechanisms that controls physiological roles of fat body cells by supporting nuclear positioning and vital secretory functions of fat body cells.

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“…They have also shown how BMs heal after injury [54,55] and how they regulate the immune response [56][57][58][59][60]. More recently, work in Drosophila has introduced a new role for BM proteins in intercellular adhesion [31].…”

Section: Introductionmentioning

confidence: 99%

“…BM is an ancient and highly conserved ECM that lines the basal surface of epithelial and endothelial tissues and surrounds muscles, adipose tissue, and nerves [26, 28,29]. Studies using Drosophila have made particularly strong contributions to our understanding of BM secretion and assembly [30][31][32][33][34][35][36][37][38][39][40][41][42][43][44][45], and the role BMs play in shaping tissues during development [35,42,[46][47][48][49][50][51][52][53]. They have also shown how BMs heal after injury [54,55] and how they regulate the immune response [56][57][58][59][60].…”

Section: Introductionmentioning

confidence: 99%

In-silicodefinition of theDrosophila melanogastermatrisome

Davis

Horne‐Badovinac

Naba

2019

Preprint

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The extracellular matrix (ECM) is an assembly of hundreds of proteins that structurally supports the cells it surrounds and biochemically regulates their functions. Drosophila has emerged as a powerful model organism to study fundamental mechanisms underlying ECM protein secretion, ECM assembly, and ECM roles in pathophysiological processes. However, as of today, we do not possess a well-defined list of the components forming the ECM of this organism. We previously reported the development of computational pipelines to define the matrisome -the ensemble of genes encoding ECM and ECM-associated proteins -of humans, mice, zebrafish and C. elegans.Using a similar approach, we report here that the Drosophila matrisome is composed of 641 genes.We further classify these genes into different structural and functional categories, including an expanded way to classify genes encoding proteins forming apical ECMs. We illustrate how having a comprehensive list of Drosophila matrisome proteins can be used to annotate large proteomic datasets and identify unsuspected roles for the ECM in pathophysiological processes. Last, to aid the dissemination and usage of the proposed definition and categorization of the Drosophila matrisome by the scientific community, our list has been made available through three public portals: The Matrisome Project, FlyBase, and GLAD.

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Inter-adipocyte Adhesion and Signaling by Collagen IV Intercellular Concentrations in Drosophila

Cited by 38 publications

References 52 publications

Collagen-binding byDrosophilaSPARC is essential for survival and for collagen IV distribution and assembly into basement membranes

Collagen-binding byDrosophilaSPARC is essential for survival and for collagen IV distribution and assembly into basement membranes

A perinuclear microtubule-organizing center controls nuclear positioning and basement membrane secretion

In-silicodefinition of theDrosophila melanogastermatrisome

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