Intracellular Trafficking Defects in Congenital Intestinal and Hepatic Diseases.
CODE
cholestasis
congenital
diarrhea
gene therapy
pediatric acute liver failure
Journal
Traffic (Copenhagen, Denmark)
ISSN: 1600-0854
Titre abrégé: Traffic
Pays: England
ID NLM: 100939340
Informations de publication
Date de publication:
Aug 2024
Aug 2024
Historique:
revised:
11
06
2024
received:
30
04
2024
accepted:
30
07
2024
medline:
27
8
2024
pubmed:
27
8
2024
entrez:
26
8
2024
Statut:
ppublish
Résumé
Enterocytes and liver cells fulfill important metabolic and barrier functions and are responsible for crucial vectorial secretive and absorptive processes. To date, genetic diseases affecting metabolic enzymes or transmembrane transporters in the intestine and the liver are better comprehended than mutations affecting intracellular trafficking. In this review, we explore the emerging knowledge on intracellular trafficking defects and their clinical manifestations in both the intestine and the liver. We provide a detailed overview including more investigated diseases such as the canonical, variant and associated forms of microvillus inclusion disease, as well as recently described pathologies, highlighting the complexity and disease relevance of several trafficking pathways. We give examples of how intracellular trafficking hubs, such as the apical recycling endosome system, the trans-Golgi network, lysosomes, or the Golgi-to-endoplasmic reticulum transport are involved in the pathomechanism and lead to disease. Ultimately, understanding these processes could spark novel therapeutic approaches, which would greatly improve the quality of life of the affected patients.
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
e12954Informations de copyright
© 2024 The Author(s). Traffic published by John Wiley & Sons Ltd.
Références
R. B. Canani, G. Castaldo, R. Bacchetta, M. G. Martín, and O. Goulet, “Congenital Diarrhoeal Disorders: Advances in This Evolving web of Inherited Enteropathies,” Nature Reviews Gastroenterology & Hepatology 12 (2015): 293–302.
J. R. Thiagarajah, D. S. Kamin, S. Acra, et al., “Advances in Evaluation of Chronic Diarrhea in Infants,” Gastroenterology 154 (2018): 2045–2059.e6.
S. J. Babcock, D. Flores‐Marin, and J. R. Thiagarajah, “The Genetics of Monogenic Intestinal Epithelial Disorders,” Human Genetics 142 (2022): 613–654.
Q. Li, Y. Sun, and S. C. D. van IJzendoorn, “A Link Between Intrahepatic Cholestasis and Genetic Variations in Intracellular Trafficking Regulators,” Biology (Basel) 10 (2021): 10.
J. E. Squires, E. M. Alonso, S. H. Ibrahim, et al., “North American Society for Pediatric Gastroenterology, Hepatology, and Nutrition Position Paper on the Diagnosis and Management of Pediatric Acute Liver Failure,” Journal of Pediatric Gastroenterology and Nutrition 74 (2022): 138–158.
A. Deep, E. C. Alexander, Y. Bulut, et al., “Advances in Medical Management of Acute Liver Failure in Children: Promoting Native Liver Survival. The Lancet Child & Adolescent,” Health 6 (2022): 725–737.
J. P. Mann, D. Lenz, Z. Stamataki, and D. Kelly, “Common Mechanisms in Pediatric Acute Liver Failure,” Trends in Molecular Medicine 29 (2022): 228–240.
S. H. Ibrahim, B. M. Kamath, K. M. Loomes, and S. J. Karpen, “Cholestatic Liver Diseases of Genetic Etiology: Advances and Controversies,” Hepatology 75 (2022): 1627–1646.
A. W. Overeem, C. Posovszky, E. H. Rings, B. N. Giepmans, and S. C. D. van IJzendoorn, “The Role of Enterocyte Defects in the Pathogenesis of Congenital Diarrheal Disorders,” Disease Models & Mechanisms 9 (2016): 1–12.
A. Treyer and A. Müsch, “Hepatocyte Polarity. Comprehensive,” Physiology 3 (2013): 243.
O. A. Weisz and E. Rodriguez‐Boulan, “Apical Trafficking in Epithelial Cells: Signals, Clusters and Motors,” Journal of Cell Science 122 (2009): 4253–4266.
I. Mellman and W. J. Nelson, “Coordinated Protein Sorting, Targeting and Distribution in Polarized Cells,” Nature Reviews Molecular Cell Biology 9 (2008): 833–845.
X. Cao, M. A. Surma, and K. Simons, “Polarized Sorting and Trafficking in Epithelial Cells,” Cell Research 22 (2012): 793–805.
P. J. Cullen and F. Steinberg, “To Degrade or Not to Degrade: Mechanisms and Significance of Endocytic Recycling,” Nature Reviews Molecular Cell Biology 19 (2018): 679–696.
G. Apodaca, L. I. Gallo, and D. M. Bryant, “Role of Membrane Traffic in the Generation of Epithelial Cell Asymmetry,” Nature Cell Biology 14 (2012): 1235–1243.
J. S. Bonifacino, “Adaptor Proteins Involved in Polarized Sorting,” Journal of Cell Biology 204 (2014): 7–17.
M. R. Golachowska, D. Hoekstra, and S. C. D. van IJzendoorn, “Recycling Endosomes in Apical Plasma Membrane Domain Formation and Epithelial Cell Polarity,” Trends in Cell Biology 20 (2010): 618–626.
I. Dingjan, P. T. Linders, D. R. Verboogen, N. H. Revelo, M. Ter Beest, and G. van den Bogaart, “Endosomal and Phagosomal SNAREs,” Physiological Reviews 98 (2018): 1465–1492.
G. P. Davidson, E. Cutz, J. R. Hamilton, and D. G. Gall, “Familial Enteropathy: A Syndrome of Protracted Diarrhea From Birth, Failure to Thrive, and Hypoplastic Villus Atrophy,” Gastroenterology 75 (1978): 783–790.
A. D. Phillips, M. Szafranski, L. Y. Man, and W. J. Wall, “Periodic Acid–Schiff Staining Abnormality in Microvillous Atrophy: Photometric and Ultrastructural Studies,” Journal of Pediatric Gastroenterology and Nutrition 30 (2000): 34–42.
N. Youssef, F. M. Ruemmele, O. Goulet, and N. Patey, “CD10 Expression in a Case of Microvillous Inclusion Disease,” Annales de Pathologie 24 (2004): 624–627.
F. M. Ruemmele, J. Schmitz, and O. Goulet, “Microvillous Inclusion Disease (Microvillous Atrophy),” Orphanet Journal of Rare Diseases 1 (2006): 1–5.
E. Cutz, J. M. Rhoads, B. Drumm, P. M. Sherman, P. R. Durie, and G. G. Forstner, “Microvillus Inclusion Disease: An Inherited Defect of Brush‐Border Assembly and Differentiation,” New England Journal of Medicine 320 (1989): 646–651.
G. F. Vogel, M. W. Hess, K. Pfaller, L. A. Huber, A. R. Janecke, and T. Müller, “Towards Understanding Microvillus Inclusion Disease,” Molecular and Cellular Pediatrics 3 (2016): 1–5.
A. Phillips and J. Schmitz, “Familial Microvillous Atrophy: A Clinicopathological Survey of 23 Cases,” Journal of Pediatric Gastroenterology and Nutrition 14 (1992): 380–396.
T. Muller, M. W. Hess, N. Schiefermeier, et al., “MYO5B Mutations Cause Microvillus Inclusion Disease and Disrupt Epithelial Cell Polarity,” Nature Genetics 40 (2008): 1163–1165.
D. M. Bowman, I. Kaji, and J. R. Goldenring, “Altered MYO5B Function Underlies Microvillus Inclusion Disease: Opportunities for Intervention at a Cellular Level,” Cellular and Molecular Gastroenterology and Hepatology 14 (2022): 553–565.
M. A. Hartman and J. A. Spudich, “The Myosin Superfamily at a Glance,” Journal of Cell Science 125 (2012): 1627–1632.
D. Aldrian, G. F. Vogel, T. K. Frey, et al., “Congenital Diarrhea and Cholestatic Liver Disease: Phenotypic Spectrum Associated With MYO5B Mutations,” Journal of Clinical Medicine 10 (2021): 10.
L. A. Lapierre, R. Kumar, C. M. Hales, et al., “Myosin VB Is Associated With Plasma Membrane Recycling Systems,” Molecular Biology of the Cell 12 (2001): 1843–1857.
J. T. Roland, A. K. Kenworthy, J. Peranen, S. Caplan, and J. R. Goldenring, “Myosin Vb Interacts With Rab8a on a Tubular Network Containing EHD1 and EHD3,” Molecular Biology of the Cell 18 (2007): 2828–2837.
J. T. Roland, L. A. Lapierre, and J. R. Goldenring, “Alternative Splicing in Class V Myosins Determines Association With Rab10,” Journal of Biological Chemistry 284 (2009): 1213–1223.
J. C. Schafer, N. W. Baetz, L. A. Lapierre, R. E. McRae, J. T. Roland, and J. R. Goldenring, “Rab11‐FIP2 Interaction With MYO5B Regulates Movement of Rab11a‐Containing Recycling Vesicles,” Traffic 15 (2014): 292–308.
D. M. Bryant, A. Datta, A. E. Rodríguez‐Fraticelli, J. Peränen, F. Martín‐Belmonte, and K. E. Mostov, “A Molecular Network for de Novo Generation of the Apical Surface and Lumen,” Nature Cell Biology 12 (2010): 1035–1045.
B. C. Knowles, J. T. Roland, M. Krishnan, et al., “Myosin Vb Uncoupling From RAB8A and RAB11A Elicits Microvillus Inclusion Disease,” Journal of Clinical Investigation 124 (2014): 2947–2962.
A. C. Engevik, I. Kaji, M. M. Postema, et al., “Loss of Myosin Vb Promotes Apical Bulk Endocytosis in Neonatal Enterocytes,” Journal of Cell Biology 218 (2019): 3647–3662.
G. F. Vogel, A. R. Janecke, I. M. Krainer, et al., “Abnormal Rab11‐Rab8‐Vesicles Cluster in Enterocytes of Patients With Microvillus Inclusion Disease,” Traffic 18 (2017): 453–464.
A. C. Engevik, I. Kaji, M. A. Engevik, et al., “Loss of MYO5B Leads to Reductions in Na+ Absorption With Maintenance of CFTR‐Dependent cl–Secretion in Enterocytes,” Gastroenterology 155 (2018): 1883–1897.e10.
C. E. Thoeni, G. F. Vogel, I. Tancevski, et al., “Microvillus Inclusion Disease: Loss of Myosin vb Disrupts Intracellular Traffic and Cell Polarity,” Traffic 15 (2014): 22–42.
A. W. Overeem, Q. Li, Y. L. Qiu, et al., “A Molecular Mechanism Underlying Genotype‐Specific Intrahepatic Cholestasis Resulting From MYO5B Mutations,” Hepatology 72 (2020): 213–229.
E. Gonzales, S. A. Taylor, A. Davit‐Spraul, et al., “MYO5B Mutations Cause Cholestasis With Normal Serum Gamma‐Glutamyl Transferase Activity in Children Without Microvillous Inclusion Disease,” Hepatology 65 (2017): 164–173.
H. S. Dhekne, O. Pylypenko, A. W. Overeem, et al., “MYO5B, STX3, and STXBP2 Mutations Reveal a Common Disease Mechanism That Unifies a Subset of Congenital Diarrheal Disorders: A Mutation Update,” Human Mutation 39 (2018): 333–344.
L. Q. van IJzendoorn SC, Q. Yl, J. S. Wang, and A. W. Overeem, “Unequal Effects of Myosin 5B Mutations in Liver and Intestine Determine the Clinical Presentation of low‐Gamma‐Glutamyltransferase Cholestasis,” Hepatology (Baltimore, MD) 72 (2020): 1461.
L. Wang, Y. L. Qiu, H. M. Xu, et al., “MYO5B‐Associated Diseases: Novel Liver‐Related Variants and Genotype‐Phenotype Correlation,” Liver International 42 (2022): 402–411.
M. Sun, O. Pylypenko, Z. Zhou, et al., “Uncovering the Relationship Between Genes and Phenotypes Beyond the Gut in Microvillus Inclusion Disease. Cellular and Molecular,” Gastroenterology and Hepatology 17 (2024): 983–1005.
M. Girard, F. Lacaille, V. Verkarre, et al., “MYO5B and Bile Salt Export Pump Contribute to Cholestatic Liver Disorder in Microvillous Inclusion Disease,” Hepatology 60 (2014): 301–310.
C. Schlegel, V. G. Weis, B. C. Knowles, et al., “Apical Membrane Alterations in Non‐intestinal Organs in Microvillus Inclusion Disease,” Digestive Diseases and Sciences 63 (2018): 356–365.
M. W. Hess, I. M. Krainer, P. A. Filipek, et al., “Advanced Microscopy for Liver and gut Ultrastructural Pathology in Patients With MVID and PFIC Caused by MYO5B Mutations,” Journal of Clinical Medicine 10 (2021): 1901.
L. Matarazzo, A. M. Bianco, E. Athanasakis, et al., “MYO5B Gene Mutations: A Not Negligible Cause of Intrahepatic Cholestasis of Infancy With Normal Gamma‐Glutamyl Transferase Phenotype,” Journal of Pediatric Gastroenterology and Nutrition 74 (2022): e115–e121.
S. Amirneni, N. Haep, M. A. Gad, A. Soto‐Gutierrez, J. E. Squires, and R. M. Florentino, “Molecular Overview of Progressive Familial Intrahepatic Cholestasis,” World Journal of Gastroenterology 26 (2020): 7470–7484.
C. L. Wiegerinck, A. R. Janecke, K. Schneeberger, et al., “Loss of Syntaxin 3 Causes Variant Microvillus Inclusion Disease,” Gastroenterology 147, no. 65–68 (2014): 65–68.e10.
G. F. Vogel, K. M. Klee, A. R. Janecke, T. Muller, M. W. Hess, and L. A. Huber, “Cargo‐Selective Apical Exocytosis in Epithelial Cells Is Conducted by Myo5B, Slp4a, Vamp7, and Syntaxin 3,” Journal of Cell Biology 211 (2015): 587–604.
A. R. Janecke, X. Liu, R. Adam, et al., “Pathogenic STX3 Variants Affecting the Retinal and Intestinal Transcripts Cause an Early‐Onset Severe Retinal Dystrophy in Microvillus Inclusion Disease Subjects,” Human Genetics 140 (2021): 1143–1156.
R. Zulliger, S. M. Conley, M. L. Mwoyosvi, M. W. Stuck, S. Azadi, and M. I. Naash, “SNAREs Interact With Retinal Degeneration Slow and rod Outer Segment Membrane Protein‐1 During Conventional and Unconventional Outer Segment Targeting,” PLoS One 10 (2015): e0138508.
J. Mazelova, N. Ransom, L. Astuto‐Gribble, M. C. Wilson, and D. Deretic, “Syntaxin 3 and SNAP‐25 Pairing, Regulated by Omega‐3 Docosahexaenoic Acid, Controls the Delivery of Rhodopsin for the Biogenesis of Cilia‐Derived Sensory Organelles, the rod Outer Segments,” Journal of Cell Science 122 (2009): 2003–2013.
R. Heidelberger, M. Kozhemyakin, J. R. Campbell, et al., “Roles of Syntaxin3 in the Inner Retina,” Investigative Ophthalmology & Visual Science 61 (2020): 3480.
M. Chograni, F. Alkuraya, I. Ourteni, F. Maazoul, I. Lariani, and H. Chaabouni, “Autosomal Recessive Congenital Cataract, Intellectual Disability Phenotype Linked to STX3 in a Consanguineous Tunisian Family,” Clinical Genetics 88 (2015): 283–287.
J. Julia, V. Shui, N. Mittal, J. Heim‐Hall, and C. L. Blanco, “Microvillus Inclusion Disease, a Diagnosis to Consider When Abnormal Stools and Neurological Impairments Run Together due to a Rare Syntaxin 3 Gene Mutation,” Journal of Neonatal‐Perinatal Medicine 12 (2019): 313–319.
B. Degar, “Familial Hemophagocytic Lymphohistiocytosis,” Hematology/Oncology Clinics 29 (2015): 903–913.
J. I. Henter, A. Horne, M. Aricó, et al., “HLH‐2004: Diagnostic and Therapeutic Guidelines for Hemophagocytic Lymphohistiocytosis,” Pediatric Blood & Cancer 48 (2007): 124–131.
J. Pagel, K. Beutel, K. Lehmberg, et al., “Distinct Mutations in STXBP2 Are Associated With Variable Clinical Presentations in Patients With Familial Hemophagocytic Lymphohistiocytosis Type 5 (FHL5),” Blood 119 (2012): 6016–6024.
P. Stepensky, J. Bartram, T. F. Barth, et al., “Persistent Defective Membrane Trafficking in Epithelial Cells of Patients With Familial Hemophagocytic Lymphohistiocytosis Type 5 Due to STXBP2/MUNC18‐2 Mutations,” Pediatric Blood & Cancer 60 (2013): 1215–1222.
G. F. Vogel, J. M. van Rijn, I. M. Krainer, et al., “Disrupted Apical Exocytosis of Cargo Vesicles Causes Enteropathy in FHL5 Patients With Munc18‐2 Mutations,” JCI Insight 2 (2017): 2.
K. Riento, T. Galli, S. Jansson, C. Ehnholm, E. Lehtonen, and V. M. Olkkonen, “Interaction of Munc‐18‐2 With Syntaxin 3 Controls the Association of Apical SNAREs in Epithelial Cells,” Journal of Cell Science 111 (1998): 2681–2688.
N. M. Dieckmann, Y. Hackmann, M. Aricò, and G. M. Griffiths, “Munc18‐2 Is Required for Syntaxin 11 Localization on the Plasma Membrane in Cytotoxic T‐Lymphocytes,” Traffic 16 (2015): 1330–1341.
W. A. Spessott, M. L. Sanmillan, M. E. McCormick, et al., “Hemophagocytic Lymphohistiocytosis Caused by Dominant‐Negative Mutations in STXBP2 That Inhibit SNARE‐Mediated Membrane Fusion,” Blood 125 (2015): 1566–1577.
M. H. Mosa, O. Nicolle, S. Maschalidi, et al., “Dynamic Formation of Microvillus Inclusions During Enterocyte Differentiation in munc18‐2–Deficient Intestinal Organoids,” Cellular and Molecular Gastroenterology and Hepatology 6 (2018): 477–493.e1.
C. Esteve, L. Francescatto, P. L. Tan, et al., “Loss‐of‐Function Mutations in UNC45A Cause a Syndrome Associating Cholestasis, Diarrhea, Impaired Hearing, and Bone Fragility,” American Journal of Human Genetics 102 (2018): 364–374.
R. Duclaux‐Loras, C. Lebreton, J. Berthelet, et al., “UNC45A Deficiency Causes Microvillus Inclusion Disease‐Like Phenotype by Impairing Myosin VB‐Dependent Apical Trafficking,” Journal of Clinical Investigation 132 (2022): 132.
Q. Li, Z. Zhou, Y. Sun, C. Sun, K. Klappe, and S. C. D. van IJzendoorn, “A Functional Relationship Between UNC45A and MYO5B Connects Two Rare Diseases With Shared Enteropathy,” Cellular and Molecular Gastroenterology and Hepatology 14 (2022): 295–310.
S. Lechuga, A. X. Cartagena‐Rivera, A. Khan, et al., “A Myosin Chaperone, UNC‐45A, Is a Novel Regulator of Intestinal Epithelial Barrier Integrity and Repair,” FASEB Journal 36 (2022): e22290.
C. F. Lee, G. C. Melkani, and S. I. Bernstein, “The UNC‐45 Myosin Chaperone: From Worms to Flies to Vertebrates,” International Review of Cell and Molecular Biology 313 (2014): 103–144.
R. Wang, Y. Wang, R. Yu, W. Xu, T. Zhang, and Y. Xiao, “Case Report: Osteo‐Oto‐Hepato‐Enteric Syndrome Caused by UNC45A Deficiency,” Frontiers in Genetics 13 (2022): 1079481.
Y. Kong, C. Ye, L. Shi, et al., “UNC45A‐Related Osteo‐Oto‐Hepato‐Enteric Syndrome in a Chinese Neonate,” European Journal of Medical Genetics 66 (2023): 104693.
R. Almaas, M. Atneosen‐Åsegg, M. E. Ytre‐Arne, et al., “Aagenaes Syndrome/Lymphedema Cholestasis Syndrome 1 Is Caused by a Founder Variant in the 5′‐Untranslated Region of UNC45A,” Journal of Hepatology 79 (2023): 945–954.
T. G. Saba, A. Montpetit, A. Verner, et al., “An Atypical Form of Erythrokeratodermia Variabilis Maps to Chromosome 7q22,” Human Genetics 116 (2005): 167–171.
A. Montpetit, S. Cote, E. Brustein, et al., “Disruption of AP1S1, Causing a Novel Neurocutaneous Syndrome, Perturbs Development of the Skin and Spinal Cord,” PLoS Genetics 4 (2008): e1000296.
K. M. C. Klee, A. R. Janecke, H. A. Civan, et al., “AP1S1 Missense Mutations Cause a Congenital Enteropathy via an Epithelial Barrier Defect,” Human Genetics 139 (2020): 1247–1259.
H. S. Alsaif, M. Al‐Owain, M. E. Barrios‐Llerena, et al., “Homozygous Loss‐of‐Function Mutations in AP1B1, Encoding Beta‐1 Subunit of Adaptor‐Related Protein Complex 1, Cause MEDNIK‐Like Syndrome,” American Journal of Human Genetics 105 (2019): 1016–1022.
D. Gravotta, A. Perez Bay, C. T. H. Jonker, et al., “Clathrin and Clathrin Adaptor AP‐1 Control Apical Trafficking of Megalin in the Biosynthetic and Recycling Routes,” Molecular Biology of the Cell 30 (2019): 1716–1728.
G. A. Castillon, P. Burriat‐Couleru, D. Abegg, N. Criado Santos, and R. Watanabe, “Clathrin and AP1 Are Required for Apical Sorting of Glycosyl Phosphatidyl Inositol‐Anchored Proteins in Biosynthetic and Recycling Routes in Madin‐Darby Canine Kidney Cells,” Traffic 19 (2018): 215–228.
P. S. Caceres, D. Gravotta, P. J. Zager, N. Dephoure, and E. Rodriguez‐Boulan, “Quantitative Proteomics of MDCK Cells Identify Unrecognized Roles of Clathrin Adaptor AP‐1 in Polarized Distribution of Surface Proteins,” Proceedings of the National Academy of Sciences of the United States of America 116 (2019): 11796–11805.
D. Martinelli, L. Travaglini, C. A. Drouin, et al., “MEDNIK Syndrome: A Novel Defect of Copper Metabolism Treatable by Zinc Acetate Therapy,” Brain 136 (2013): 872–881.
P. Gissen, C. A. Johnson, N. V. Morgan, et al., “Mutations in VPS33B, Encoding a Regulator of SNARE‐Dependent Membrane Fusion, Cause Arthrogryposis‐Renal Dysfunction‐Cholestasis (ARC) syndrome,” Nature Genetics 36 (2004): 400–404.
A. R. Cullinane, A. Straatman‐Iwanowska, A. Zaucker, et al., “Mutations in VIPAR Cause an Arthrogryposis, Renal Dysfunction and Cholestasis Syndrome Phenotype With Defects in Epithelial Polarization,” Nature Genetics 42 (2010): 303–312.
A. Spang, “Membrane Tethering Complexes in the Endosomal System,” Frontiers in Cell and Development Biology 4 (2016): 35.
M. R. Hunter, G. G. Hesketh, T. H. Benedyk, A. C. Gingras, and S. C. Graham, “Proteomic and Biochemical Comparison of the Cellular Interaction Partners of Human VPS33A and VPS33B,” Journal of Molecular Biology 430 (2018): 2153–2163.
C. Rogerson and P. Gissen, “VPS33B and VIPAR Are Essential for Epidermal Lamellar Body Biogenesis and Function,” Biochimica et Biophysica Acta ‐ Molecular Basis of Disease 1864 (2018): 1609–1621.
B. Xiang, G. Zhang, S. Ye, et al., “Characterization of a Novel Integrin Binding Protein, VPS33B, Which Is Important for Platelet Activation and in Vivo Thrombosis and Hemostasis,” Circulation 132 (2015): 2334–2344.
J. Hanley, D. K. Dhar, F. Mazzacuva, et al., “Vps33b Is Crucial for Structural and Functional Hepatocyte Polarity,” Journal of Hepatology 66 (2017): 1001–1011.
B. Banushi, F. Forneris, A. Straatman‐Iwanowska, et al., “Regulation of Post‐Golgi LH3 Trafficking Is Essential for Collagen Homeostasis,” Nature Communications 7 (2016): 12111.
T. B. Haack, C. Staufner, M. G. Kopke, et al., “Biallelic Mutations in NBAS Cause Recurrent Acute Liver Failure With Onset in Infancy,” American Journal of Human Genetics 97 (2015): 163–169.
M. A. Cousin, E. Conboy, J. S. Wang, et al., “RINT1 Bi‐Allelic Variations Cause Infantile‐Onset Recurrent Acute Liver Failure and Skeletal Abnormalities,” American Journal of Human Genetics 105 (2019): 108–121.
D. Lenz, P. McClean, A. Kansu, et al., “SCYL1 Variants Cause a Syndrome With low Gamma‐Glutamyl‐Transferase Cholestasis, Acute Liver Failure, and Neurodegeneration (CALFAN),” Genetics in Medicine 20 (2018): 1255–1265.
C. Staufner, B. Peters, M. Wagner, et al., “Defining Clinical Subgroups and Genotype‐Phenotype Correlations in NBAS‐Associated Disease Across 110 Patients,” Genetics in Medicine 22 (2020): 610–621.
T. Aoki, S. Ichimura, A. Itoh, et al., “Identification of the Neuroblastoma‐Amplified Gene Product as a Component of the Syntaxin 18 Complex Implicated in Golgi‐To‐Endoplasmic Reticulum Retrograde Transport,” Molecular Biology of the Cell 20 (2009): 2639–2649.
M. Tagaya, K. Arasaki, H. Inoue, and H. Kimura, “Moonlighting Functions of the NRZ (Mammalian Dsl1) complex,” Frontiers in Cell and Development Biology 2 (2014): 25.
Y. Ren, C. K. Yip, A. Tripathi, et al., “A Structure‐Based Mechanism for Vesicle Capture by the Multisubunit Tethering Complex Dsl1,” Cell 139 (2009): 1119–1129.
S. Zink, D. Wenzel, C. A. Wurm, and H. D. Schmitt, “A Link Between ER Tethering and COP‐I Vesicle Uncoating,” Developmental Cell 17 (2009): 403–416.
K. Arasaki, M. Taniguchi, K. Tani, and M. Tagaya, “RINT‐1 Regulates the Localization and Entry of ZW10 to the Syntaxin 18 Complex,” Molecular Biology of the Cell 17 (2006): 2780–2788.
D. Longman, K. A. Jackson‐Jones, M. M. Maslon, et al., “Identification of a Localized Nonsense‐Mediated Decay Pathway at the Endoplasmic Reticulum,” Genes & Development 34 (2020): 1075–1088.
X. Lin, C. C. Liu, Q. Gao, X. Zhang, G. Wu, and W. H. Lee, “RINT‐1 Serves as a Tumor Suppressor and Maintains Golgi Dynamics and Centrosome Integrity for Cell Survival,” Molecular and Cellular Biology 27 (2007): 4905–4916.
L. J. Kong, A. R. Meloni, and J. R. Nevins, “The Rb‐Related p130 Protein Controls Telomere Lengthening Through an Interaction With a Rad50‐Interacting Protein, RINT‐1,” Molecular Cell 22 (2006): 63–71.
K. Arasaki, D. Takagi, A. Furuno, et al., “A New Role for RINT‐1 in SNARE Complex Assembly at the Trans‐Golgi Network in Coordination With the COG Complex,” Molecular Biology of the Cell 24 (2013): 2907–2917.
J. L. Burman, L. Bourbonniere, J. Philie, et al., “Scyl1, Mutated in a Recessive Form of Spinocerebellar Neurodegeneration, Regulates COPI‐Mediated Retrograde Traffic,” Journal of Biological Chemistry 283 (2008): 22774–22786.
J. N. Hamlin, L. K. Schroeder, M. Fotouhi, et al., “Scyl1 Scaffolds Class II Arfs to Specific Subcomplexes of Coatomer Through the Gamma‐COP Appendage Domain,” Journal of Cell Science 127 (2014): 1454–1463.
G. Amano, S. Matsuzaki, Y. Mori, et al., “SCYL1 Arginine Methylation by PRMT1 Is Essential for Neurite Outgrowth Via Golgi Morphogenesis,” Molecular Biology of the Cell 31 (2020): 1963–1973.
H. Farhan, M. W. Wendeler, S. Mitrovic, et al., “MAPK Signaling to the Early Secretory Pathway Revealed by Kinase/Phosphatase Functional Screening,” Journal of Cell Biology 189 (2010): 997–1011.
J. L. Burman, J. N. Hamlin, and P. S. McPherson, “Scyl1 Regulates Golgi Morphology,” PLoS One 5 (2010): e9537.
C. Staufner, T. B. Haack, M. G. Kopke, et al., “Recurrent Acute Liver Failure Due to NBAS Deficiency: Phenotypic Spectrum, Disease Mechanisms, and Therapeutic Concepts,” Journal of Inherited Metabolic Disease 39 (2016): 3–16.
F. M. Ruemmele, T. Müller, N. Schiefermeier, et al., “Loss‐of‐Function of MYO5B Is the Main Cause of Microvillus Inclusion Disease: 15 Novel Mutations and a CaCo‐2 RNAi Cell Model,” Human Mutation 31 (2010): 544–551.
T. Sato, R. G. Vries, H. J. Snippert, et al., “Single Lgr5 Stem Cells Build Crypt‐Villus Structures in Vitro Without a Mesenchymal Niche,” Nature 459 (2009): 262–265.
M. Kalashyan, K. Raghunathan, H. Oller, et al., “Patient‐Derived Enteroids Provide a Platform for the Development of Therapeutic Approaches in Microvillus Inclusion Disease,” Journal of Clinical Investigation 133 (2023): e169234.
A. Burman, M. Momoh, L. Sampson, et al., “Modeling of a Novel Patient‐Based MYO5B Point Mutation Reveals Insights Into MVID Pathogenesis,” Cellular and Molecular Gastroenterology and Hepatology 15 (2023): 1022–1026.
I. Kaji, J. T. Roland, M. Watanabe, et al., “Lysophosphatidic Acid Increases Maturation of Brush Borders and SGLT1 Activity in MYO5B‐Deficient Mice, a Model of Microvillus Inclusion Disease,” Gastroenterology 159 (2020): 1390–1405.e20.
I. Kaji, J. T. Roland, S. Rathan‐Kumar, et al., “Cell Differentiation Is Disrupted by MYO5B Loss Through Wnt/Notch Imbalance,” JCI Insight 6 (2021): 6.
N. Zabaleta, C. Unzu, N. D. Weber, and G. Gonzalez‐Aseguinolaza, “Gene Therapy for Liver Diseases—Progress and Challenges,” Nature Reviews Gastroenterology & Hepatology 20 (2023): 1–18.
S. Maestro, N. D. Weber, N. Zabaleta, R. Aldabe, and G. Gonzalez‐Aseguinolaza, “Novel Vectors and Approaches for Gene Therapy in Liver Diseases,” JHEP Reports 3 (2021): 100300.
M. F. Naso, B. Tomkowicz, W. L. Perry, III, and W. R. Strohl, “Adeno‐Associated Virus (AAV) as a Vector for Gene Therapy,” BioDrugs 31 (2017): 317–334.
R. J. Thompson, R. Artan, U. Baumann, et al., “Interim Results From an Ongoing, Open‐Label, Single‐Arm Trial of Odevixibat in Progressive Familial Intrahepatic Cholestasis,” JHEP Reports 5 (2023): 100782.
K. M. Loomes, R. H. Squires, D. Kelly, et al., “Maralixibat for the Treatment of PFIC: Long‐Term, IBAT Inhibition in an Open‐Label, Phase 2 Study,” Hepatology Communications 6 (2022): 2379–2390.
K. J. van der Velde, H. S. Dhekne, M. A. Swertz, et al., “An Overview and Online Registry of Microvillus Inclusion Disease Patients and Their MYO5B Mutations,” Human Mutation 34 (2013): 1597–1605.
K. M. Klee, M. W. Hess, M. Lohmüller, et al., “A CRISPR‐Screen in Intestinal Epithelial Cells Identifies Novel Factors for Polarity and Apical Transport,” eLife 12 (2023): e80135.