Related Experiment Video

Updated: Feb 5, 2026

Extraction and Quantification of Soluble, Radiolabeled Inositol Polyphosphates from Different Plant Species using SAX-HPLC
09:01

Extraction and Quantification of Soluble, Radiolabeled Inositol Polyphosphates from Different Plant Species using SAX-HPLC

Published on: June 26, 2020

7.6K

Inositol polyphosphate 4-phosphatase type II regulation of androgen receptor activity

Manqi Zhang1, Egla Suarez2, Judy L Vasquez2

  • 1Department of Chemistry and Biochemistry, Florida International University, Miami, FL, 33199, USA.

Oncogene
|September 20, 2018
PubMed

Insights

Loss of INPP4B, a tumor suppressor, impacts androgen receptor (AR) activity and oncogenic signaling in prostate cancer. Restoring INPP4B may offer new therapeutic strategies for advanced prostate cancer.

Area of Science:

  • Oncology
  • Molecular Biology
  • Genetics

Background:

  • Androgen receptor (AR) signaling is crucial in prostate cancer progression.
  • Loss of tumor suppressors INPP4B and PTEN is linked to AR activation in advanced prostate cancer.
  • The role of INPP4B in AR regulation remains unclear.

Purpose of the Study:

  • To investigate the role of INPP4B in regulating AR activity and associated signaling pathways.
  • To determine if INPP4B loss contributes to AR-dependent transcriptional profiles in prostate cancer.

Main Methods:

  • Utilized prostate cancer cell lines to assess INPP4B's effect on AR transcriptional activity, Akt, and PKC signaling.
  • Analyzed gene expression data from prostate cancer patient cohorts.
  • Employed an Inpp4b knockout (Inpp4b-/-) mouse model to study INPP4B's function in normal prostate tissue.

Main Results:

  • INPP4B was found to regulate AR transcriptional activity, Akt, and PKC signaling in prostate cancer cells.
  • A positive correlation was observed between INPP4B expression and AR mRNA levels/transcriptional output in patient cohorts.
  • In Inpp4b-/- mice, INPP4B loss suppressed Akt and PKC signaling and modulated AR transcriptional activity without affecting PTEN levels.

Conclusions:

  • INPP4B plays a significant role in modulating AR activity in normal prostate epithelium.
  • Loss of INPP4B contributes to the AR-dependent transcriptional reprogramming observed in prostate cancer.
  • INPP4B is a potential therapeutic target for managing advanced prostate cancer.

More Related Videos

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases06:56

Author Spotlight: Developing Tools to Tune the Activity of Tyrosine Phosphatases

Published on: September 6, 2024

815
Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation09:04

Detection of Neu1 Sialidase Activity in Regulating TOLL-like Receptor Activation

Published on: September 7, 2010

12.0K

Related Concept Videos

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.1K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.5K
Internal Receptors01:31

Internal Receptors

Many cellular signals are hydrophilic and therefore cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind to internal, or intracellular, receptors that reside within the cell. Many mammalian steroid hormones use this mechanism of cell signaling, as does nitric oxide (NO) gas.
74.7K
Types of Receptors: Internal Receptors01:07

Types of Receptors: Internal Receptors

Many cellular signals are hydrophilic and cannot pass through the plasma membrane. However, small or hydrophobic signaling molecules can cross the hydrophobic core of the plasma membrane and bind intracellular receptors that reside within the cell cytoplasm or nucleus. Many mammalian steroid hormones and nitric oxide (NO) gas use this cell signaling mechanism.
Similar to membrane-bound receptors, the binding of a ligand to the intracellular receptor of causes a conformational change in the...
32.6K
Types of Receptors: Cell Surface Receptors01:28

Types of Receptors: Cell Surface Receptors

Cell-surface receptors, also known as transmembrane receptors, are cell surface, membrane-anchored (integral) proteins that bind to external ligand molecules. This type of receptor spans the plasma membrane and performs signal transduction, converting an extracellular signal into an intracellular signal. Ligands that interact with cell-surface receptors do not have to enter the cell that they affect. Cell-surface receptors are also called cell-specific proteins or markers because they are...
27.4K
GTPases and their Regulation02:14

GTPases and their Regulation

Guanine nucleotide-binding proteins (G-proteins), also known as GTPases, are a superfamily of proteins that regulate many cellular processes, such as cell signaling, vesicular transport, and the regulation of cell shape and motility. Mutation or dysfunction of these proteins can lead to disease. There are around 40,000 known G-proteins that can broadly be classified into two groups ‒  small G-proteins consisting of a single domain and large multi-domain G-proteins.
Large G-proteins,...
9.9K