Loss of INPP5K attenuates IP3-induced Ca2+ responses in the glioblastoma cell line U-251 MG cells

Loncke, Jens; Luyten, Tomas; Ramos, Ana Raquel; Erneux, Christophe; Bultynck, Geert

doi:10.1016/j.bbadva.2023.100105

Cited by 1 publication

(1 citation statement)

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“…While a large pool localizes to the ER, INPP5K can be recruited to the plasma membrane to downregulate PI(3,4,5)P 3 signaling upon growth factor stimulation (Gurung et al, 2003). In Caenorhabditis elegans, INPP5K together with atlastin-1 was shown to be involved in maintaining the non-uniform, somatodendritic enrichment of neuronal ER/plasma membrane contacts in their soma and dendrites, which are mostly absent in axons (Loncke et al, 2023). The hypoglycosylation of dystroglycan in patients with INPP5K loss-of-function further connects INPP5K with ER and Golgi functions.…”

Section: Discussionmentioning

confidence: 99%

Knockdown of INPP5K compromises the differentiation of N2A cells

Manzolillo,

Gresing,

Hübner

et al. 2024

Front. Mol. Neurosci.

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Inositol polyphosphate 5-phosphatase K (INPP5K), also known as SKIP (skeletal muscle and kidney-enriched inositol phosphatase), is a cytoplasmic enzyme with 5-phosphatase activity toward phosphoinositides (PIs). Mutations in INPP5K are associated with autosomal recessive congenital muscular dystrophy with cataracts and intellectual disability (MDCCAID). Notably, muscular dystrophy is characterized by the hypoglycosylation of dystroglycan. Thus, far, the underlying mechanisms are only partially understood. In this study, we show that INPP5K expression increases during brain development. Knockdown of INPP5K in the neuroblastoma-derived cell line N2A impaired their neuronal-like differentiation and interfered with protein glycosylation.

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Section: Discussionmentioning

confidence: 99%