Dataset Information

Arylsulfatase L (ARSL) Controls Glycosaminoglycan Sulfation During Skeletal Development

ABSTRACT: Proteoglycans are essential components of the cartilage extracellular matrix (ECM), with glycosaminoglycan (GAG) chains playing a crucial role in skeletal development. This study identifies a previously unknown substrate of arylsulfatase L (ARSL) a Golgi-localized enzyme. To investigate ARSL’s physiological substrate, the study utilized the TurboID proximity labeling approach. TurboID, a biotin ligase, biotinylates interacting proteins, allowing their isolation via streptavidin beads and identification through mass spectrometry (MS). We generated RCS (Rat chondrosarcoma) cells overexpressing FLAG-TurboID-Arsl, confirming its Golgi localization. MS analysis revealed 129 significantly enriched proteins in ARSL-labeled samples, with gene ontology (GO) analysis highlighting extracellular matrix organization. Among these proteins, Acan, a precursor of Aggrecan—rich in sulfated GAGs—was identified as a key ARSL interactor, reinforcing the enzyme’s role in ECM regulation and skeletal development.

INSTRUMENT(S):

ORGANISM(S): Rattus Norvegicus (rat)

TISSUE(S): Permanent Cell Line Cell, Cell Culture

SUBMITTER: Marianna Maddaluno

LAB HEAD: Carmine Settembre

PROVIDER: PXD061172 | Pride | 2026-06-15

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	2020-02-03_GDT_MM_RCSTurboID_RCSTURBO_1.raw	Raw
	2020-02-03_GDT_MM_RCSTurboID_RCSTURBO_2.raw	Raw
	2020-02-03_GDT_MM_RCSTurboID_RCSTURBO_3.raw	Raw
	2020-02-03_GDT_MM_RCSTurboID_RCSTURBO_4.raw	Raw
	2020-02-03_GDT_MM_RCSTurboID_RCSTURBO_B_1.raw	Raw

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Publications

Arylsulfatase L is a Golgi chondroitin sulfatase regulating skeletal development.

Maddaluno Marianna M De Leonibus Chiara C Del Prete Eugenio E Salierno Francesco Giuseppe FG Intartaglia Daniela D Carrella Diego D Conte Ivan I Volpi Nicola N Settembre Carmine C

The Journal of biological chemistry 20260506 6

Sulfatases are a family of enzymes that hydrolyze sulfate esters from various substrates. Defects, in sulfatase activity, are associated with various human diseases due to the accumulation of sulfated substrates. Deficiency in ARSL, a Golgi sulfatase, is associated with X-linked recessive chondrodysplasia punctata (CDPX), a disorder characterized by defects in cartilage and bone development. However, until now, ARSL function has remained unknown. In this study, we demonstrate that ARSL promotes ...[more]

PMID: 42103217

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