GOLGA1

Last updated
GOLGA1
Protein KIFC3 PDB 2h58.png
Identifiers
Aliases GOLGA1 , golgin-97, golgin A1
External IDs OMIM: 602502 MGI: 1924149 HomoloGene: 68223 GeneCards: GOLGA1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_002077

NM_001290649
NM_029793

RefSeq (protein)

NP_002068

NP_001277578
NP_084069

Location (UCSC) Chr 9: 124.88 – 124.95 Mb Chr 2: 38.91 – 38.96 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Golgin subfamily A member 1 is a protein that in humans is encoded by the GOLGA1 gene. [5] [6]

Contents

The Golgi apparatus, which participates in glycosylation and transport of proteins and lipids in the secretory pathway, consists of a series of stacked cisternae (flattened membrane sacs). Interactions between the Golgi and microtubules are thought to be important for the reorganization of the Golgi after it fragments during mitosis. The golgins are a family of proteins, of which the protein encoded by this gene is a member, that are localized to the Golgi. This encoded protein is associated with Sjogren's syndrome. [6]

Interactions

GOLGA1 has been shown to interact with ARL1. [7]

Related Research Articles

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<span class="mw-page-title-main">GRASP55</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">Giantin</span> Protein-coding gene in the species Homo sapiens

Giantin or Golgin subfamily B member 1 is a protein that in humans is encoded by the GOLGB1 gene. Giantin is located at the cis-medial rims of the Golgi apparatus and is part of the Golgi matrix that is responsible for membrane trafficking in secretory pathway of proteins. This function is key for proper localisation of proteins at the plasma membrane and outside the cell which is important for cell function that is dependent on for example receptors and the extracellular matrix function. Recent animal model knockout studies of GOLGB1 in mice, rat, and zebrafish have shown that phenotypes are different between species ranging from mild to severe craniofacial defects in the rodent models to just minor size defects in zebrafish. However, in adult zebrafish a tumoral calcinosis-like phenotype was observed, and in humans such phenotype has been linked to defective glycosyltransferase function.

<span class="mw-page-title-main">Golgi matrix</span>

The Golgi matrix is a collection of proteins involved in the structure and function of the Golgi apparatus. The matrix was first isolated in 1994 as an amorphous collection of 12 proteins that remained associated together in the presence of detergent and 150 mM NaCl. Treatment with a protease enzyme removed the matrix, which confirmed the importance of proteins for the matrix structure. Modern freeze etch electron microscopy (EM) clearly shows a mesh connecting Golgi cisternae and associated vesicles. Further support for the existence of a matrix comes from EM images showing that ribosomes are excluded from regions between and near Golgi cisternae.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000136935 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026754 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Griffith KJ, Chan EK, Lung CC, Hamel JC, Guo X, Miyachi K, Fritzler MJ (September 1997). "Molecular cloning of a novel 97-kd Golgi complex autoantigen associated with Sjögren's syndrome". Arthritis and Rheumatism. 40 (9): 1693–1702. doi: 10.1002/art.1780400920 . PMID   9324025.
  6. 1 2 "Entrez Gene: GOLGA1 golgi autoantigen, golgin subfamily a, 1".
  7. Lu L, Hong W (September 2003). "Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi". Molecular Biology of the Cell. 14 (9): 3767–3781. doi:10.1091/mbc.E03-01-0864. PMC   196566 . PMID   12972563.

Further reading