GDPD5

Last update 08 May 2025

Basic Info

Synonyms

GDE2, GDPD5, Glycerophosphocholine phosphodiesterase GDPD5

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Introduction

Glycerophosphodiester phosphodiesterase that promotes neurite formation and drives spinal motor neuron differentiation (By similarity). Mediates the cleavage of glycosylphosphatidylinositol (GPI) anchor of target proteins: removes the GPI-anchor of RECK, leading to release RECK from the plasma membrane (By similarity). May contribute to the osmotic regulation of cellular glycerophosphocholine (By similarity).

100 Clinical Results associated with GDPD5

100 Translational Medicine associated with GDPD5

0 Patents (Medical) associated with GDPD5

Literatures (Medical) associated with GDPD5

01 Feb 2025·The Plant Journal

Phosphate deficiency inducible OsGDPD5 affects root growth by regulating sugar‐auxin crosstalk

Article

Author: Verma, Lokesh ; Singh, Bhagat ; Giri, Jitender ; Pandey, Mandavi ; Bhatia, Chitra ; Mehra, Poonam

SUMMARYGlycerophosphodiester phosphodiesterases (GDPDs) enzymes are known to be involved in phospholipids degradation pathways, where glycerophosphodiesters are hydrolyzed to glycerol‐3‐phosphate (G3P) and corresponding alcohol. In plants, GDPDs are involved in phosphate deficiency adaptive responses and have been shown to impact root length, but the precise mechanism remains unclear. This study focuses on the rice GDPD5 gene and its role in regulating primary root growth. Our research demonstrates that OsGDPD5 encodes a functional GDPD enzyme and could hydrolyze glycerophosphocholine and glycerophosphorylethanolamine. At transcriptional levels, OsGDPD5 is preferentially expressed in the root tip and regulated by transcription factor OsPHR2. We have used CRISPR/Cas9 to generate OsGDPD5 knock‐out lines, allowing us to explore its role in root growth. Our findings show that osgdpd5 mutants had a shorter primary root, which could be restored to a normal level by the exogenous application of sugar or G3P. Further, knocking out OsGDPD5 alters endogenous levels of G3P and sugars, affecting auxin biosynthesis in the root and, ultimately, primary root growth. In this manner, OsGDPD5 has a crucial role in regulating physiological processes, specifically sugar and auxin signaling, which are known to be involved in root growth regulation in rice. Our research thus unraveled a link between rice phosphate deficiency‐responsive lipid remodeling and root growth via sugar‐hormone signaling.

04 Sep 2024·Cancer Research

PRKDC Induces Chemoresistance in Osteosarcoma by Recruiting GDE2 to Stabilize GNAS and Activate AKT

Article

Author: Li, Zhihong ; Yin, Chi ; Zhang, Wenchao ; Jin, Xin ; Feng, Chengyao ; Xu, Haodong ; Liu, Binfeng ; Tu, Chao ; Li, Wei

AbstractChemoresistance is one of the major causes of poor prognosis in osteosarcoma. Alternative therapeutic strategies for osteosarcoma are limited, indicating that increasing sensitivity to currently used chemotherapies could be an effective approach to improve patient outcomes. Using a kinome-wide CRISPR screen, we identified PRKDC as a critical determinant of doxorubicin (DOX) sensitivity in osteosarcoma. The analysis of clinical samples demonstrated that PRKDC was hyperactivated in osteosarcoma, and functional experiments showed that the loss of PRKDC significantly increased sensitivity of osteosarcoma to DOX. Mechanistically, PRKDC recruited and bound GDE2 to enhance the stability of protein GNAS. The elevated GNAS protein levels subsequently activated AKT phosphorylation and conferred resistance to DOX. The PRKDC inhibitor AZD7648 and DOX synergized and strongly suppressed the growth of osteosarcoma in mouse xenograft models and human organoids. In conclusion, the PRKDC-GDE2-GNAS-AKT regulatory axis suppresses DOX sensitivity and comprises targetable candidates for improving the efficacy of chemotherapy in osteosarcoma.Significance: Targeting PRKDC suppresses AKT activation and increases sensitivity to doxorubicin in osteosarcoma, which provides a therapeutic strategy for overcoming chemoresistance.

01 Sep 2024·The FEBS Journal

KLF7 promotes neuroblastoma differentiation through the GTPase signaling pathway by upregulating neuroblast differentiation‐associated protein AHNAKs and glycerophosphodiesterase GDPD5

Article

Author: Shi, Lei ; Song, Yue ; Xia, Yang ; Xie, Li ; Zhang, Xue ; Song, Huilin ; Zhang, Jiahui ; Jia, Ying ; Jing, Wenwen ; Meng, Lingdi ; Cao, Tianhua ; Qiao, Shupei

The arrest of neural crest‐derived sympathoadrenal neuroblast differentiation contributes to neuroblastoma formation, and overriding this blocked differentiation is a clear strategy for treating high‐risk neuroblastoma. A better understanding of neuroblast or neuroblastoma differentiation is essential for developing new therapeutic approaches. It has been proposed that Krueppel‐like factor 7 (KLF7) is a neuroblastoma super‐enhancer‐associated transcription factor gene. Moreover, KLF7 was found to be intensely active in postmitotic neuroblasts of the developing nervous system during embryogenesis. However, the role of KLF7 in the differentiation of neuroblast or neuroblastoma is unknown. Here, we find a strong association between high KLF7 expression and favorable clinical outcomes in neuroblastoma. KLF7 induces differentiation of neuroblastoma cells independently of the retinoic acid (RA) pathway and acts cooperatively with RA to induce neuroblastoma differentiation. KLF7 alters the GTPase activity and multiple differentiation‐related genes by binding directly to the promoters of neuroblast differentiation‐associated protein (AHNAK and AHNAK2) and glycerophosphodiester phosphodiesterase domain‐containing protein 5 (GDPD5) and regulating their expression. Furthermore, we also observe that silencing KLF7 in neuroblastoma cells promotes the adrenergic‐to‐mesenchymal transition accompanied by changes in enhancer‐mediated gene expression. Our results reveal that KLF7 is an inducer of neuroblast or neuroblastoma differentiation with prognostic significance and potential therapeutic value.

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GDPD5

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