GOLGA2: A Potential Drug Target and Biomarker for Golgi Disorders

Target Name: GOLGA2

NCBI ID: G2801

GOLGA2

GOLGA2: A Potential Drug Target and Biomarker for Golgi Disorders

Introduction

Golgi are a type of intracellular organ that plays a crucial role in the proper functioning of cells. They are responsible for the synthesis, modification, and delivery of proteins, as well as the degradation of damaged or unnecessary proteins. The Golgi system is composed of several components, including the transmembrane proteins that form the Golgi membrane, the cytoplasmic proteins that interact with the membrane, and the proteins that traffic between the membrane and the cytoplasm. One of the proteins that plays a crucial role in the Golgi system is GOLGA2, a 130 kDa cis-Golgi matrix protein.

GOLGA2: Structure and Function

GOLGA2 is a member of the GOLGENES family of transmembrane proteins. It consists of a single open-loop alpha-helical transmembrane protein that contains a unique N-terminal region that is rich in conserved secondary structure. The N-terminal region of GOLGA2 contains a 100 amino acid long N-terminal domain that is characterized by a putative transmembrane domain, a 25 amino acid long cytoplasmic domain, and a 35 amino acid long C-terminal domain.

The cytoplasmic domain of GOLGA2 is rich in conserved structural features, including a conserved alpha-helix and a conserved beta-sheet. The alpha-helical transmembrane region of GOLGA2 is characterized by a unique arrangement of 12 conserved amino acids at its N-terminus. This arrangement is thought to play a role in the protein's stability and its ability to interact with other components of the Golgi system.

GOLGA2 is involved in several critical processes in the Golgi system, including the formation of the Golgi membrane, the sorting of proteins into the membrane, and the regulation of protein traffic between the membrane and the cytoplasm. It is also involved in the degradation of damaged or unnecessary proteins, which is thought to play a role in the regulation of cellular homeostasis.

GOLGA2 has also been shown to be involved in several diseases, including neurodegenerative disorders, cancer, and autoimmune diseases. For example, studies have shown that GOLGA2 is overexpressed in several neurodegenerative disorders, including Alzheimer's disease and Parkinson's disease. This suggests that GOLGA2 may be a potential drug target for these disorders.

GOLGA2 has also been shown to be involved in the regulation of cancer cell growth and metastasis. For example, studies have shown that GOLGA2 is overexpressed in several types of cancer, including breast, ovarian, and prostate cancer. This suggests that GOLGA2 may be a potential biomarker for cancer and may be a target for anti-cancer drugs.

GOLGA2 has also been shown to be involved in the regulation of autoimmune diseases. For example, studies have shown that GOLGA2 is overexpressed in several autoimmune diseases, including rheumatoid arthritis and multiple sclerosis. This suggests that GOLGA2 may be a potential drug target for these diseases.

Drug Targeting Strategies

GOLGA2 is a protein that has the potential to be a drug target due to its unique structure and function in the Golgi system. There are several potential strategies that could be used to target GOLGA2, including:

1. Antibody-based therapies: One potential approach to targeting GOLGA2 is to use antibodies to block its function.

Protein Name: Golgin A2

Functions: Peripheral membrane component of the cis-Golgi stack that acts as a membrane skeleton that maintains the structure of the Golgi apparatus, and as a vesicle thether that facilitates vesicle fusion to the Golgi membrane (Probable) (PubMed:16489344). Required for normal protein transport from the endoplasmic reticulum to the Golgi apparatus and the cell membrane (By similarity). Together with p115/USO1 and STX5, involved in vesicle tethering and fusion at the cis-Golgi membrane to maintain the stacked and inter-connected structure of the Golgi apparatus. Plays a central role in mitotic Golgi disassembly: phosphorylation at Ser-37 by CDK1 at the onset of mitosis inhibits the interaction with p115/USO1, preventing tethering of COPI vesicles and thereby inhibiting transport through the Golgi apparatus during mitosis (By similarity). Also plays a key role in spindle pole assembly and centrosome organization (PubMed:26165940). Promotes the mitotic spindle pole assembly by activating the spindle assembly factor TPX2 to nucleate microtubules around the Golgi and capture them to couple mitotic membranes to the spindle: upon phosphorylation at the onset of mitosis, GOLGA2 interacts with importin-alpha via the nuclear localization signal region, leading to recruit importin-alpha to the Golgi membranes and liberate the spindle assembly factor TPX2 from importin-alpha. TPX2 then activates AURKA kinase and stimulates local microtubule nucleation. Upon filament assembly, nascent microtubules are further captured by GOLGA2, thus linking Golgi membranes to the spindle (PubMed:19242490, PubMed:26165940). Regulates the meiotic spindle pole assembly, probably via the same mechanism (By similarity). Also regulates the centrosome organization (PubMed:18045989, PubMed:19109421). Also required for the Golgi ribbon formation and glycosylation of membrane and secretory proteins (PubMed:16489344, PubMed:17314401)

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The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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