ArticleThe EMBO journal2000
Transmembrane transforming growth factor-alpha tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55.
Article in The EMBO journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 115 citations in OpenAlex.
- Identification and evaluation of Pharmacological enhancers of the factor VII p.Q160R variant.Scientific reports · 2025Article
- Amino acid and protein specificity of protein fatty acylation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- An mTORC1-GRASP55 signaling axis controls unconventional secretion to reshape the extracellular proteome upon stress.Molecular cell · 2021Article
- Adaptation of the Golgi Apparatus in Cancer Cell Invasion and Metastasis.Frontiers in cell and developmental biology · 2021Review
- The protein secretion modulator TMED9 drives CNIH4/TGFα/GLI signaling opposing TMED3-WNT-TCF to promote colon cancer metastases.Oncogene · 2019Article
- Golgi Structure and Function in Health, Stress, and Diseases.Results and problems in cell differentiation · 2019Review
- New Insights Into the Golgi Stacking Proteins.Frontiers in cell and developmental biology · 2019Review
- Human rhomboid family-1 modulates clathrin coated vesicle-dependent pro-transforming growth factor α membrane trafficking to promote breast cancer progression.EBioMedicine · 2018Article
- Protein Lipidation: Occurrence, Mechanisms, Biological Functions, and Enabling Technologies.Chemical reviews · 2018Article
- TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators.Autophagy · 2018Article
- Land-locked mammalian Golgi reveals cargo transport between stable cisternae.Nature communications · 2017Article
- Genetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis.PLoS genetics · 2017Article
- Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45.The Journal of biological chemistry · 2017Article
- Golgi structure formation, function, and post-translational modifications in mammalian cells.F1000Research · 2017Review
- New structural insights into Golgi Reassembly and Stacking Protein (GRASP) in solution.Scientific reports · 2016Article
- GRASPs in Golgi Structure and Function.Frontiers in cell and developmental biology · 2015Review
- Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly.Biology open · 2012Article
- Epidermal growth factor cytoplasmic domain affects ErbB protein degradation by the lysosomal and ubiquitin-proteasome pathway in human cancer cells.Neoplasia (New York, N.Y.) · 2012Article
- Structure of Golgi transport proteins.Cold Spring Harbor perspectives in biology · 2011Review
- Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Transforming growth factor-alpha (TGF-alpha) and related proteins represent a family of transmembrane growth factors with representatives in flies and worms. Little is known about the transport of TGF-alpha and other transmembrane growth factors to the cell surface and its regulation. p59 was purified as a cytoplasmic protein, which at endogenous levels associates with transmembrane TGF-alpha. cDNA cloning of p59 revealed a 452 amino acid sequence with two PDZ domains. p59 is myristoylated and palmitoylated, and associates with the Golgi system, where it co-localizes with TGF-alpha. Its first PDZ domain interacts with the C-terminus of transmembrane TGF-alpha and select transmembrane proteins. p59 is the human homolog of GRASP55, which is structurally related to GRASP65. GRASP55 and GRASP65 have been shown to play a role in stacking of the Golgi cisternae in vitro. C-terminal mutations of transmembrane TGF-alpha, which decrease or abolish the interaction with p59, also strongly impair cell surface expression of TGF-alpha. Our observations suggest a role for membrane tethering of p59/GRASP55 to select transmembrane proteins, including TGF-alpha, in maturation and transport to the cell surface.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.