PIP4P1

Last update 08 May 2025

Basic Info

Synonyms

C14orf9, MGC26684, phosphatidylinositol-4,5-bisphosphate 4-phosphatase 1

+ [6]

Introduction

Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (PubMed:16365287). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (PubMed:16365287). Regulates lysosomal positioning by recruiting JIP4 to lysosomal membranes, thus inducing retrograde transport of lysosomes along microtubules (PubMed:29146937). Contributes to assembly of the V-ATPase complex in lipid rafts of the lysosomal membrane and to subsequent amino acid-dependent activation of mTORC1 (PubMed:29644770). May play a role in the regulation of cellular cholesterol metabolism (PubMed:25035345).

100 Clinical Results associated with PIP4P1

100 Translational Medicine associated with PIP4P1

0 Patents (Medical) associated with PIP4P1

Literatures (Medical) associated with PIP4P1

14 Jun 2024·Biological and Pharmaceutical Bulletin

CRISPRa Analysis of Phosphoinositide Phosphatases Shows That TMEM55A Is a Positive Regulator of Autophagy

Article

Author: Fukushima, Yu ; Shimada, Chinatsu ; Nomura, Wataru ; Matsumoto, Daisuke ; Nigorikawa, Kiyomi

Transcriptional activation, based on Clustered regularly interspaced short palindromic repeats (CRISPR)-CRISPR-associated protein 9 (Cas9) and known as CRISPR activation (CRISPRa), is a specific and safe tool to upregulate endogenous genes. Therefore, CRISPRa is valuable not only for analysis of molecular mechanisms of cellular events, but also for treatment of various diseases. Regulating autophagy has been proposed to enhance effects of some therapies. In this study, we upregulated genes for phosphoinositide phosphatases, SACM1L, PIP4P1, and PIP4P2, using CRISPRa, and their effects on autophagy were examined. Our results suggested that TMEM55A/PIP4P2, a phosphatidylinositol-4,5-bisphosphate 4-phosphatase, positively regulates basal autophagy in 293A cells. Furthermore, it was also suggested that SAC1, a phosphatidylinositol 4-phosphatase, negatively regulates basal autophagic degradation.

01 Jan 2024·Hippocampus

Hippocampal TMEM55B overexpression in the 5XFAD mouse model of Alzheimer's disease

Article

Author: Odfalk, Kristian F. ; Dobrowolski, Radek ; Smith, Sabrina ; Hopp, Sarah C. ; Wickline, Jessica L.

AbstractDysfunction of the endosomal‐lysosomal network is a notable feature of Alzheimer's disease (AD) pathology. Dysfunctional endo‐lysosomal vacuoles accumulate in dystrophic neurites surrounding amyloid β (Aβ) plaques and may be involved in the pathogenesis and progression of Aβ aggregates. Trafficking and thus maturation of these dysfunctional vacuoles is disrupted in the vicinity of Aβ plaques. Transmembrane protein 55B (TMEM55B), also known as phosphatidylinositol‐4,5‐bisphosphate 4‐phosphatase 1 (PIP4P1) is an endo‐lysosomal membrane protein that is necessary for appropriate trafficking of endo‐lysosomes. The present study tested whether overexpression of TMEM55B in the hippocampus could prevent plaque‐associated axonal accumulation of dysfunctional endo‐lysosomes, reduce Aβ plaque load, and prevent hippocampal‐dependent learning and memory deficits in the 5XFAD mouse models of Aβ plaque pathology. Immunohistochemical analyses revealed a modest but significant reduction in the accumulation of endo‐lysosomes in dystrophic neurites surrounding Aβ plaques, but there was no change in hippocampal‐dependent memory or plaque load. Overall, these data indicate a potential role for TMEM55B in reducing endo‐lysosomal dysfunction during AD‐like Aβ pathology.

15 Dec 2023·Science Advances

Parkinson’s VPS35[D620N] mutation induces LRRK2-mediated lysosomal association of RILPL1 and TMEM55B

Article

Author: Phung, Toan K. ; Jaimon, Ebsy ; Dickie, Emily A. ; Nirujogi, Raja S. ; Taylor, Matthew ; Lam, Pui Yiu ; Fasimoye, Rotimi ; Macartney, Thomas ; Tonelli, Francesca ; Yeshaw, Wondwossen M. ; Wightman, Melanie ; Hecht, Chloe A. ; Pfeffer, Suzanne R. ; Pal, Prosenjit ; Lis, Pawel ; Alessi, Dario R.

We demonstrate that the Parkinson’s VPS35[D620N] mutation alters the expression of ~220 lysosomal proteins and stimulates recruitment and phosphorylation of Rab proteins at the lysosome. This recruits the phospho-Rab effector protein RILPL1 to the lysosome where it binds to the lysosomal integral membrane protein TMEM55B. We identify highly conserved regions of RILPL1 and TMEM55B that interact and design mutations that block binding. In mouse fibroblasts, brain, and lung, we demonstrate that the VPS35[D620N] mutation reduces RILPL1 levels, in a manner reversed by LRRK2 inhibition and proteasome inhibitors. Knockout of RILPL1 enhances phosphorylation of Rab substrates, and knockout of TMEM55B increases RILPL1 levels. The lysosomotropic agent LLOMe also induced LRRK2 kinase–mediated association of RILPL1 to the lysosome, but to a lower extent than the D620N mutation. Our study uncovers a pathway through which dysfunctional lysosomes resulting from the VPS35[D620N] mutation recruit and activate LRRK2 on the lysosomal surface, driving assembly of the RILPL1-TMEM55B complex.

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PIP4P1

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