Golgi membrane protein 1 Antibodies

Golgi membrane protein 1 (GOLM1)

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Cellular response protein to viral infection.

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Gene Information

Human
Gene Name:	GOLM1
Uniprot:	Q8NBJ4
Entrez:	51280

Family

Belongs to:
GOLM1/CASC4 family

Alternative Names

bA379P1.3; FLJ23608; golgi membrane protein 1; Golgi membrane protein GP73; Golgi phosphoprotein 2C9orf155; golgi protein, 73-kD; GOLPH2 FLJ22634; GP73 chromosome 9 open reading frame 155; GP73; PSEC0257

Molecular Weight

Mass (kDA):
45.333 kDA

Genomic Context

Human
Location:	9q21.33
Sequence:	9; NC_000009.12 (86026141..86100201, complement)

Tissue Specificity

Widely expressed. Highly expressed in colon, prostate, trachea and stomach. Expressed at lower level in testis, muscle, lymphoid tissues, white blood cells and spleen. Predominantly expressed by cells of the epithelial lineage. Expressed at low level in normal liver. Expression significantly increases in virus (HBV, HCV) infected liver. Expression does not increase in liver disease due to non-viral causes (alcohol-induced liver disease, autoimmune hepatitis). Increased expression in hepatocytes appears to be a general feature of advanced liver disease. In liver tissue from patients with adult giant-cell hepatitis (GCH), it is strongly expressed in hepatocytes-derived syncytial giant cells. Constitutively expressed by biliary epithelial cells but not by hepatocytes.

Subcellular Localizations

Golgi apparatus, cis-Golgi network membrane; Single-pass type II membrane protein. Early Golgi. Cycles via the cell surface and endosomes upon lumenal pH disruption.

Diseases

• Liver Carcinoma
• Carcinoma
• Liver Neoplasms
• Malignant Neoplasms
• Neoplasms
• Hepatitis
• Liver Diseases
• Liver Cirrhosis
• Malignant Neoplasm Of Prostate
• Prostatic Neoplasms
• Hepatitis B
• Hepatitis, Chronic
• Malignant Paraganglionic Neoplasm

• Fibrosis
• Neoplasm Metastasis
• Adenocarcinoma
• Hepatitis B, Chronic
• Malignant Neoplasm Of Liver
• Alzheimer's Disease
• Focal Nodular Hyperplasia

Interacting Proteins

• EGFR

Pathways

• Localization
• Secretion
• Transport
• Golgi Localization
• Glycosylation
• Fucosylation
• Protein Secretion
• Pronephros Development
• Reverse Transcription

• Cell Differentiation
• Bone Development
• Golgi Organization
• Pathogenesis

PTMs

• Glycosylation

• Cleavage

Research Areas

• Golgi Apparatus Markers
• Signal Transduction

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/GOLM1

Best Uses of the GOLM1 Marker

This article will cover the GOLPH3L, GOLPH3L, and GOLPH3R proteins. It will also discuss how they interact with cytoplasmictails of a subset Golgi -localized modification enzymes. GOLPH2 can also be used as a molecular marker for cancer. We'll also discuss the use of GOLPH3 as a paralogue.

GOLPH3 interacts to cytoplasmic ends of a subset Golgi enzymes

A subset from the Golgi proteases interacts with GOLPH3 using their cytoplasmic heads. GOLPH3 clients and GALNT2 clients share one common trait: they both have an enrichment of positively charged substances. A similar amino acid composition is shared by both clients: the tails for both proteins contain six to seven positively-charged residues.

GOLPH3 interactions with chimeras using different enzymatic pathways were tested. The chimeras consisted of proteins whose respective cytoplasmic tails were derived via the O-linked glycosylation pathways GNPTAB or mucin-type O.linked glycosylation pathways. This study did not include the ST6GAL1 protein.

GOLPH3 coated cytoplasmic heads of a number Golgi protein-resident proteins have an acidic patch conserved near the TMD. It indicates that the cytoplasmic bodies are less of six to ten residues long. The GOLPH3/GOLPH3L structure shows that the protein contains leucine residues as its second most abundant residues, which is consistent with reports of a L-x-R/K motif.

GOLPH3L was identified using affinity chromatography. These proteins were able to enrich a wide variety of proteins, including Golgi resident Glycosylation enzymes as well as all COPI coat subunits. Immunoblotting also confirmed the enrichment of GALNT7, b-COP.

Although biochemical data about the interaction of GOLPH3 to ERD1 are not yet available, they indicate a functional relationship between GOLPH3 client enzymes and GOLPH3. Their interaction with VPS74 could also be biochemically tested using the Y2H method. In the meantime we are waiting for dedicated experiments that will test the effects of Erd1 on these two proteins.

Recent studies have shown ERD1 as well as GOLPH3 are necessary for the retention of a subset GolgI proteins. These enzymes are recycled in yeast via a COPI dependent pathway mediated mainly by Ent1 (Dop1) and Ent5. GOLPH3 & Erd1 also mediate two distinct intra-Golgi recycling pathways.

These results indicate that GOLPH3L and GOLPH3L interact with different levels of cytoplasmic tails. Both mechanisms play a role in the retention of Golgi-resident enzymes. GOLPH3 interacts with Golgi-resident enzymes' cytoplasmic ends. They also demonstrate that GOLPH3L, and GOLPH3L interacts avec the cytoplasmic heads of a subset Golgi-resident enzymes.

These interactions could also influence intra-Golgi recycle and glycosylation. It may also affect the composition the glycome cancer cells. Further studies will reveal the role of the axis in glycosylation. Further studies are required to determine the mechanism by which GOLPH3L acts to regulate glycosylation.

GOLPH3 undergoes extensive post-translational modification, including phosphorylation and ubiquitination. Its activity has a physiologically variable control. GOLPH3 is a key drug target for cancers that are resistant to conventional therapies. GOLPH3 regulates the dynamics of client enzymes.

GOLPH3L interacts cytoplasmic Tails of a Paralogue

Although there are many great uses for the GOLM1 markers, there are a few key conditions. Medulloblastoma is one of these conditions. Congenital malformations and cataracts are another. Eye anomalies like microphthalmia or coloboma are also listed. Online, you can find a complete list of GOLM1-marker applications.

GOLPH2 can be used as a molecular biomarker for cancer

Recent research has identified GOLPH2 protein as a potential biomarker for cancer. GOLPH2 levels were higher than those of other biomarkers like PSA, PCA3, or AMACR. GOLPH2 was also found in cancer tissues to be higher than normal tissue. Its levels were upregulated for about 90% of cases. This biomarker can also help determine if patients are candidates for chemotherapy.

Golgi phosphoprotein 2 is a type II Golgi antigen. This antigen is expressed in various epithelial cells, including the prostate. Although its function is not fully understood, it is often overexpressed in prostate cancer specimens. However, the BosterBio GOLPH2 may be used as molecular biomarkers for cancer.

Biomarker discovery has increased due to the rapid advancement of biotechnologies. Currently, researchers are reporting several biomarkers that show great promise. Several biomarkers are currently being further investigated to validate them. While existing discovery methods identify many candidate markers in each investigation, only a small number make it to clinical phase. This means that there's still much to do.

Up until now, doctors relied only on the presence of symptoms in cancer patients. They can now use biomarkers to determine the type of cancer. A single blood sample can determine if the cancer has minimal residual or resistance to certain drugs. These biomarkers allow doctors to determine which patients need aggressive care.

Prostate cancer is the most common form of malignancy among American men. African Americans are particularly at risk. Early diagnosis is essential. Current biomarkers of prostate cancer are not very useful because they fail to distinguish between aggressive or indolent forms. A lot of current biomarkers don't distinguish between aggressive or non-aggressive forms.

When biomarker tests are performed alongside specific cancer treatments, they are known as companion diagnostic tests. These tests are different to genetic testing which is used for determining if someone inherits certain mutations from one's parents. These results are used to help doctors decide the most effective treatment for a particular patient. Some therapies, such a targeted chemotherapy or immunotherapy can only work with particular biomarkers.