Glycolipid transfer protein knockout disrupts vesicle trafficking to the plasma membrane
The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It has been proposed to act as a sensor and regulator of glycosphingolipid homeostasis in cells. Furthermore, through its previously determined...
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| Published in | The Journal of biological chemistry Vol. 299; no. 4; p. 104607 |
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| Main Authors | , , , , , , |
| Format | Journal Article |
| Language | English |
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United States
Elsevier Inc
01.04.2023
American Society for Biochemistry and Molecular Biology |
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| Abstract | The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It has been proposed to act as a sensor and regulator of glycosphingolipid homeostasis in cells. Furthermore, through its previously determined interaction with the endoplasmic reticulum membrane protein VAP-A (vesicle-associated membrane protein-associated protein A), GLTP may also be involved in facilitating vesicular transport in cells. In this study, we characterized the phenotype of CRISPR/Cas9-mediated GLTP KO HeLa cells. We showed that motility, three-dimensional growth, and cellular metabolism were all altered by GLTP knockout. Expression of a GLTP mutant incapable of binding VAP disrupted cell spheroid formation, indicating that the GLTP–VAP interaction is linked to cellular adhesion, cohesion, and three-dimensional growth. Most notably, we found evidence that GLTP, through its interaction with VAP-A, affects vesicular trafficking, marking the first cellular process discovered to be directly impacted by a change in GLTP expression. |
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| AbstractList | The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It has been proposed to act as a sensor and regulator of glycosphingolipid homeostasis in cells. Furthermore, through its previously determined interaction with the endoplasmic reticulum membrane protein VAP-A (vesicle-associated membrane protein-associated protein A), GLTP may also be involved in facilitating vesicular transport in cells. In this study, we characterized the phenotype of CRISPR/Cas9-mediated GLTP KO HeLa cells. We showed that motility, three-dimensional growth, and cellular metabolism were all altered by GLTP knockout. Expression of a GLTP mutant incapable of binding VAP disrupted cell spheroid formation, indicating that the GLTP-VAP interaction is linked to cellular adhesion, cohesion, and three-dimensional growth. Most notably, we found evidence that GLTP, through its interaction with VAP-A, affects vesicular trafficking, marking the first cellular process discovered to be directly impacted by a change in GLTP expression. The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It has been proposed to act as a sensor and regulator of glycosphingolipid homeostasis in cells. Furthermore, through its previously determined interaction with the endoplasmic reticulum membrane protein VAP-A (vesicle-associated membrane protein-associated protein A), GLTP may also be involved in facilitating vesicular transport in cells. In this study, we characterized the phenotype of CRISPR/Cas9-mediated GLTP KO HeLa cells. We showed that motility, three-dimensional growth, and cellular metabolism were all altered by GLTP knockout. Expression of a GLTP mutant incapable of binding VAP disrupted cell spheroid formation, indicating that the GLTP–VAP interaction is linked to cellular adhesion, cohesion, and three-dimensional growth. Most notably, we found evidence that GLTP, through its interaction with VAP-A, affects vesicular trafficking, marking the first cellular process discovered to be directly impacted by a change in GLTP expression. The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It has been proposed to act as a sensor and regulator of glycosphingolipid homeostasis in cells. Furthermore, through its previously determined interaction with the endoplasmic reticulum membrane protein VAP-A (vesicle-associated membrane protein-associated protein A), GLTP may also be involved in facilitating vesicular transport in cells. In this study, we characterized the phenotype of CRISPR/Cas9-mediated GLTP KO HeLa cells. We showed that motility, three-dimensional growth, and cellular metabolism were all altered by GLTP knockout. Expression of a GLTP mutant incapable of binding VAP disrupted cell spheroid formation, indicating that the GLTP-VAP interaction is linked to cellular adhesion, cohesion, and three-dimensional growth. Most notably, we found evidence that GLTP, through its interaction with VAP-A, affects vesicular trafficking, marking the first cellular process discovered to be directly impacted by a change in GLTP expression.The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It has been proposed to act as a sensor and regulator of glycosphingolipid homeostasis in cells. Furthermore, through its previously determined interaction with the endoplasmic reticulum membrane protein VAP-A (vesicle-associated membrane protein-associated protein A), GLTP may also be involved in facilitating vesicular transport in cells. In this study, we characterized the phenotype of CRISPR/Cas9-mediated GLTP KO HeLa cells. We showed that motility, three-dimensional growth, and cellular metabolism were all altered by GLTP knockout. Expression of a GLTP mutant incapable of binding VAP disrupted cell spheroid formation, indicating that the GLTP-VAP interaction is linked to cellular adhesion, cohesion, and three-dimensional growth. Most notably, we found evidence that GLTP, through its interaction with VAP-A, affects vesicular trafficking, marking the first cellular process discovered to be directly impacted by a change in GLTP expression. |
| ArticleNumber | 104607 |
| Author | Mattjus, Peter Backman, Anders P.E. Blom, Tomas Lönnfors, Max Nurmi, Henrik Halin, Josefin Roos-Mattjus, Pia |
| Author_xml | – sequence: 1 givenname: Henrik orcidid: 0000-0002-9747-8662 surname: Nurmi fullname: Nurmi, Henrik organization: Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland – sequence: 2 givenname: Anders P.E. orcidid: 0000-0001-8144-4030 surname: Backman fullname: Backman, Anders P.E. organization: Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland – sequence: 3 givenname: Josefin orcidid: 0000-0002-0125-469X surname: Halin fullname: Halin, Josefin organization: Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland – sequence: 4 givenname: Max orcidid: 0000-0002-3655-9733 surname: Lönnfors fullname: Lönnfors, Max organization: Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland – sequence: 5 givenname: Tomas orcidid: 0000-0001-9711-8387 surname: Blom fullname: Blom, Tomas organization: Department of Anatomy and Research Programs Unit, Faculty of Medicine, University of Helsinki, Helsinki, Finland – sequence: 6 givenname: Pia orcidid: 0000-0002-7187-2012 surname: Roos-Mattjus fullname: Roos-Mattjus, Pia organization: Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland – sequence: 7 givenname: Peter orcidid: 0000-0001-8991-5933 surname: Mattjus fullname: Mattjus, Peter email: peter.mattjus@abo.fi organization: Department of Biochemistry, Faculty of Science and Engineering, Åbo Akademi University, Turku, Finland |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36924944$$D View this record in MEDLINE/PubMed |
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| Keywords | GLTP glycolipid VAP-A VAP sphingolipid VSVG gene silencing lipid transport GO intracellular trafficking glycerosphingolipid ER gRNA DMEM GSLs Golgi cDNA endoplasmic reticulum (ER) ERES MCS OCR |
| Language | English |
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| Snippet | The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It... The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It... The glycolipid transfer protein (GLTP) has been linked to many cellular processes aside from its best-known in vitro function as a lipid transport protein. It... |
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| SubjectTerms | Biological Transport - genetics Carrier Proteins - genetics Carrier Proteins - metabolism Cell Membrane - metabolism Cell Movement - genetics Cytosol - metabolism endoplasmic reticulum (ER) Gene Expression Regulation - genetics Gene Knockout Techniques gene silencing glycerosphingolipid glycolipid Golgi HeLa Cells Humans intracellular trafficking lipid transport Protein Binding - genetics sphingolipid VAP-A VSVG |
| Title | Glycolipid transfer protein knockout disrupts vesicle trafficking to the plasma membrane |
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