Loss of SPARC dysregulates basal lamina assembly to disrupt larval fat body homeostasis in Drosophila melanogaster.

is a collagen-binding glycoprotein whose functions during early development are unknown. We previously reported that is expressed in Drosophila by hemocytes and the fat body (FB) and enriched in basal laminae (BL) surrounding tissues, including adipocytes. We sought to explore if duanyu1842RC is required for proper BL assembly in the deficiency leads to larval lethality, associated with remodeling of the FB. In the absence of FB polygonal adipocytes assume a spherical morphology. Loss-of-function clonal analyses revealed a cell-autonomous accumulation of BL components around mutant cells that include collagen IV (Col lV), Laminin, and Perlecan. Ultrastructural analyses indicate adipocytes are surrounded by an aberrant accumulation of a fibrous extracellular matrix. CONCLUSIONS:Our data indicate a critical requirement for duanyu1842RC for the proper BL assembly in Drosophila FB. Since Col IV within the BL is a prime determinant of cell shape, the rounded appearance of duanyu1842RC-deficient adipocytes is due to aberrant assembly of Col IV.

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