Cited by 181Sphingolipid Metabolism and SignalingLysosomal Storage Disorders ResearchLipid metabolism and biosynthesis

The DOI matches its Crossref record; 21 of the 22 references it cites were found in a registry or an index.

TRAM, LAG1 and CLN8: members of a novel family of lipid-sensing domains?

Winter, Eitan, Ponting, Chris P·2002·Trends in Biochemical Sciences

Open this paper in CoChat — free account

Abstract

A family of membrane-associated proteins related to yeast Lag1p and mammalian TRAM has been identified. The family includes the protein product of CLN8, a gene mutated in progressive epilepsy with mental retardation. Mouse CLN8 is also mutated in the mnd/mnd mouse, a model for neuronal ceroid lipofuscinoses. The identification of these homologues has potential implications for our understanding of ceramide synthesis, lipid regulation and protein translocation in the endoplasmic reticulum.

Integrity signals

Registry

Crossref · 10.1016/s0968-0004(02)02154-0

Cites

21 of 21 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

A comprehensive two-hybrid analysis to explore the yeast protein interactome
Ito, T., Chiba, T., Ozawa, R., Yoshida, M., Hattori, M., & Sakaki, Y. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.061034498 · Cited by 3,566
Improving the accuracy of PSI-BLAST protein database searches with composition-based statistics and other refinements
Schäffer, A. A. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.14.2994 · Cited by 1,375
Sterol regulatory element-binding proteins (SREBPs): transcriptional regulators of lipid synthetic genes
Shimano, H. (2001) · Progress in Lipid Research · doi:10.1016/s0163-7827(01)00010-8 · Cited by 763
Topology prediction for helical transmembrane proteins at 86% accuracy–Topology prediction at 86% accuracy
Rost, B., Fariselli, P., & Casadio, R. (1996) · Protein Science · doi:10.1002/pro.5560050824 · Cited by 608
TRAPP, a highly conserved novel complex on the cis‐Golgi that mediates vesicle docking and fusion
Sacher, M., Jiang, Y., Barrowman, J., Scarpa, A., Burston, J., Zhang, L., Schieltz, D., Yates, J. R., Abeliovich, H., & Ferro-Novick, S. (1998) · EMBO Journal · doi:10.1093/emboj/17.9.2494 · Cited by 326
The neuronal ceroid lipofuscinoses in human EPMR and mnd mutant mice are associated with mutations in CLN8
Ranta, S., Zhang, Y., Ross, B., Lonka, L., Takkunen, E., Messer, A. C., Sharp, J. D., Wheeler, R. B., Kusumi, K., Mole, S., et al. (1999) · Nature Genetics · doi:10.1038/13868 · Cited by 319
The sterol-sensing domain: multiple families, a unique role?
Kuwabara, P. E., & Labouesse, M. (2002) · Trends in Genetics · doi:10.1016/s0168-9525(02)02640-9 · Cited by 285
Upstream of Growth and Differentiation Factor 1 (uog1), a Mammalian Homolog of the Yeast Longevity Assurance Gene 1 (LAG1), RegulatesN-Stearoyl-sphinganine (C18-(Dihydro)ceramide) Synthesis in a Fumonisin B1-independent Manner in Mammalian Cells
Venkataraman, K., Riebeling, C., Bodennec, J., Riezman, H., Allegood, J. C., Sullards, M. C., Merrill, A. H., & Futerman, A. H. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m205211200 · Cited by 282
C26‐CoA‐dependent ceramide synthesis of Saccharomyces cerevisiae is operated by Lag1p and Lac1p
Guillas, I., Kirchman, P. A., Chuard, R., Pfefferli, M., Jiang, J. C., Jazwinski, S. M., & Conzelmann, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.11.2655 · Cited by 277
Lag1p and Lac1p Are Essential for the Acyl-CoA–dependent Ceramide Synthase Reaction inSaccharomyces cerevisae
Schorling, S., Vallée, B., Barz, W. P., Riezman, H., & Oesterhelt, D. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.11.3417 · Cited by 276

Show all 22 references

Sorted by citations

Items 101–181 of 181

Neuronal ceroid lipofuscinosis in Salukis is caused by a single base pair insertion in CLN8
Lingaas, F., Guttersrud, O., Arnet, E. F., & Espenes, A. (2018) · Animal Genetics · doi:10.1111/age.12629 · Cited by 19
The neuronal ceroid-lipofuscinoses (Batten disease)
Mole, S., & Schulz, A. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19176-3.00018-2 · Cited by 19
Mechanism of ceramide synthase inhibition by fumonisin B1
Zhang, Z., Fang, Q., Xie, T., & Gong, X. (2024) · Structure · doi:10.1016/j.str.2024.06.002 · Cited by 21
Identification of a novel brain‐specific and reelin‐regulated gene that encodes a protein colocalized with synapsin
Kuvbachieva, A. A., Lepagnol-Bestel, A.-M., Tissir, F., Maloum, I., Guimiot, F., Ramoz, N., Bourgeois, F., Moalic, J., Goffinet, A. M., & Simonneau, M. (2004) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2004.03473.x · Cited by 17
“The LAG1 (for ‘longevity-assurance protein’) domain is a putative lipid-sensing domain found in a variety of membrane-associated proteins (Jazwinski & Conzelmann, 2002; Winter & Ponting, 2002).”
Background
TRAM-LAG1-CLN8 family proteins are acyltransferases regulating phospholipid composition
Sheokand, P. K., James, A. M., Jenkins, B., Lysyganicz, P. K., Lacabanne, D., King, M. S., Kunji, E. R. S., Siniossoglou, S., Koulman, A., Murphy, M. P., et al. (2025) · Science Advances · doi:10.1126/sciadv.adr3723 · Cited by 17
“S1A) ( 6 ).”
Neuronal ceroid lipofuscinosis related ER membrane protein CLN8 regulates PP2A activity and ceramide levels
Adhikari, B., Silva, B. D., Molina, J. A., Allen, A., Peck, S. H., & Lee, S. Y. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.11.011 · Cited by 17
Molecular Cloning, Characterisation and Tissue-specific Expression of Human LAG3, a Member of the Novel Lag1 Protein Family
Cai, X.-F., Tao, Z., Yan, Z., Yang, S., & Gong, Y. (2003) · DNA sequence · doi:10.1080/1042517021000041831 · Cited by 16
“Most of the homologue proteins share a similar profile of six or seven transmembrane helices, a basic domain between the first two helices on the amino terminus, a Lag1 motif of 52 amino acids and a carboxyl-terminal acidic domain (Jiang et al., 1998; Winter and Ponting, 2002).”
Background
Gene expression profiling in vLINCL CLN6-deficient fibroblasts: Insights into pathobiology
Teixeira, C. A., Lin, S. M., Mangas, M., Quinta, R., Bessa, C., Ferreira, C., Sá-Miranda, C., Boustany, R., & Ribeiro, G. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.002 · Cited by 16
Pathogenicity-associated protein domains: The fiercely-conserved evolutionary signatures
Patel, S. V. (2017) · Gene Reports · doi:10.1016/j.genrep.2017.04.004 · Cited by 17
“lipid regulation and neural processes (Winter and Ponting, 2002).”
Background
Innovations in Antifungal Drug Discovery among Cell Envelope Synthesis Enzymes through Structural Insights
Zhou, Y., & Reynolds, T. B. (2024) · Journal of Fungi · doi:10.3390/jof10030171 · Cited by 18
Ceramide synthases in mammalians, worms, and insects: emerging schemes
Voelzmann, A., & Bauer, R. (2010) · BioMolecular Concepts · doi:10.1515/bmc.2010.028 · Cited by 15
CLN8 Mutations Presenting with a Phenotypic Continuum of Neuronal Ceroid Lipofuscinosis—Literature Review and Case Report
Badura‐Stronka, M., Winczewska‐Wiktor, A., Pietrzak, A., Hirschfeld, A. S., Żemojtel, T., Wołyńska, K., Bednarek-Rajewska, K., Seget, M., Matheisel, A., Latos‐Bieleńska, A., et al. (2021) · Genes · doi:10.3390/genes12070956 · Cited by 14
Genome-Wide Association Study Reveals Key Genes for Differential Lead Accumulation and Tolerance in Natural Arabidopsis thaliana Accessions
Busoms, S., Pérez‐Martín, L., Llimós, M., Poschenrieder, C., & Martos, S. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.689316 · Cited by 15
“TRAM/LAG1/CLN8 lipid-sensing domain has been well described in humans and yeast, where it is associated with ER-Golgi trafficking (Winter and Ponting, 2002).”
Background
Identification of TRAMs as sphingolipid-binding proteins using a photoactivatable and clickable short-chain ceramide analog
Deng, Y., You, L., Lu, Y. D., Han, S., Wang, J., Vicas, N., Chen, C., & Ye, J. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101415 · Cited by 14
“Both TRAM proteins and ceramide synthase contain a TLC domain that was postulated to bind ceramide or related sphingolipids (14).”
Background
Molecular and functional characterization of the ceramide synthase from Trypanosoma cruzi
Figueiredo, J. M., Rodrigues, D. C., Silva, R. C. M. C., Koeller, C. M., Jiang, J. C., Jazwinski, S. M., Previato, J. O., Mendonça‐Previato, L., Ürményi, T. P., & Heise, N. (2011) · Molecular and Biochemical Parasitology · doi:10.1016/j.molbiopara.2011.12.006 · Cited by 14
“The putative T. cruzi CerS gene (TcCERS1) was previously identified as a TLC member, a family of membrane-associated proteins with lipid-sensing domains related to human TRAM, yeast Lag1p and mammalian CLN8 [76].”
BackgroundInfluential
Cloning and characterization of a LASS1-GDF1 transcript in rat cerebral cortex: Conservation of a bicistronic structure
Wang, B.-H., Shi, G., Fu, Y.-C., & Xu, X. (2007) · DNA sequence · doi:10.1080/10425170601060947 · Cited by 13
“RPS-BLAST program revealed that the deduced amino acid sequence contains a Lag1p motif and a TLC domain of five predicted transmembrane alpha helices conserved in Lag1p, Tram, and Cln8 (SMART accession number SM0724) ER membrane associated proteins (Winter and Ponting 2002).”
Ceramide Synthases: Reexamining Longevity
Park, J., & Pewzner‐Jung, Y. (2013) · Handbook of experimental pharmacology · doi:10.1007/978-3-7091-1368-4_5 · Cited by 13
Congenital ichthyosis in Prader–Willi syndrome associated with maternal chromosome 15 uniparental disomy: Case report and review of autosomal recessive conditions unmasked by UPD
Muthusamy, K., Macke, E. L., Klee, E. W., Tebben, P. J., Hand, J. L., Hasadsri, L., Marcou, C. A., & Schimmenti, L. A. (2020) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.61792 · Cited by 13
“This motif contains two conserved histidine residues thought to play a role in substrate binding (Mizutani et al., 2006; Winter & Ponting, 2002).”
Background
Bioinformatic perspectives in the neuronal ceroid lipofuscinoses
Kmoch, S., Stránecký, V., Emes, R. D., & Mitchison, H. M. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2012.12.010 · Cited by 12
CLN 8 disease caused by large genomic deletions
Beesley, C. E., Guerreiro, R. J., Brás, J., Williams, R. E., Taratuto, A. L., Eltze, C. M., & Mole, S. (2016) · Molecular Genetics & Genomic Medicine · doi:10.1002/mgg3.263 · Cited by 11
The mevalonate pathway: a monitoring approach in plants by systems biology tools
Bhangu-Uhlmann, A. (2011) · Repository for Publications and Research Data (ETH Zurich) · doi:10.3929/ethz-a-006690303 · Cited by 11
Phosphorylated LASS2 inhibits prostate carcinogenesis via negative regulation of Wnt/β‐catenin signaling
Zhang, K., Wu, R., Mei, F., Zhou, Y., He, L., Liu, Y., Zhao, X., You, J., Liu, B., Meng, Q., et al. (2021) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29926 · Cited by 10
Identification of Potential Proteinaceous Ligands of GI.1 Norovirus in Pacific Oyster Tissues
Lyu, C., Li, J., Shi, Z., An, R., Wang, Y., Luo, G., & Wang, D. (2023) · Viruses · doi:10.3390/v15030631 · Cited by 9
“The IFT has the TRAM–Lag1p–CLN8 (TLC) domain, which as four p ssible functions: catalyzing the syn sis of ceramide-like moieti s or activating lipid synthesis, protect ng proteins from proteolysis, lipid tran port ng, a d acting as lipid se sors [33].”
Background
Identification and Expression Analysis of the Zebrafish Homologs of the ceramide synthase Gene Family
Brondolin, M., Berger, S., Reinke, M., Tanaka, H., Ohshima, T., Fuβ, B., & Hoch, M. (2012) · Developmental Dynamics · doi:10.1002/dvdy.23913 · Cited by 9
“The catalytic activity of all Cers resides in the Lag1 motif, a stretch of 52 amino acids (Spassieva et al., 2006), which localizes within the TLC (Tram, Lag and CLN8) domain, a region of approximately 200 C-terminal residues (Winter and Ponting, 2002).”
Ylpex5 mutation partially suppresses the defective hyphal growth of a Yarrowia lipolytica ceramide synthase mutant, Yllac1, by recovering lipid raft polarization and vacuole morphogenesis
Bal, J., Lee, H., Cheon, S. A., Lee, K. J., Oh, D., & Kim, J. (2012) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2012.11.003 · Cited by 9
Common Variation Neighbouring Micro-RNA 22 Is Associated with Increased Left Ventricular Mass
Harper, A. R., Mayosi, B. M., Rodríguez, A., Rahman, T., Hall, D. H., Mamasoula, C., Avery, P. J., & Keavney, B. D. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055061 · Cited by 9
“The function of TLCD2 is unknown, however it has been postulated that it may have a role in both lipid metabolism and ceramide synthesis [11].”
Functional Analysis of the Ceramide Synthase Gene ALT7, A Homolog of the Disease Resistance Gene Asc1, in the Plant Pathogen Alternaria alternata
Kheder, A. A., & Akagi, Y. (2012) · Journal of Plant Pathology & Microbiology · doi:10.4172/2157-7471.s2-001 · Cited by 8
“Predicted transmembrane domains of TLC-containing proteins are also found in Alt7 (Figure 1C) [23,24].”
BackgroundInfluential
Structure of the yeast ceramide synthase
Schäfer, J.-H., Clausmeyer, L., Körner, C., Esch, B. M., Wolf, V. N., Sapia, J., Ahmed, Y., Walter, S., Vanni, S., Januliene, D., et al. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01415-2 · Cited by 10
“Notably, two adjacent histidine residues are conserved in the CerS family required for catalytic activity 25,37 .”
LASS5 Interacts with SDHB and Synergistically Represses p53 and p21 Activity
Jiang, Z., Li, F., Wan, Y., Han, Z., Yuan, W., Cao, L., Deng, Y., Peng, X., Chen, F., Fan, X., et al. (2016) · Current Molecular Medicine · doi:10.2174/1566524016666160607090012 · Cited by 7
“LASS5 contains a DNAbinding HOX domain involved in transcriptional regulation and a TLC-motif, characteristic of family members, that includes five membrane-spanning helices [31, 32].”
Background
Ceramide synthase homolog Tlc4 maintains nuclear envelope integrity via its Golgi translocation
Hirano, Y., Ohno, Y., Kubota, Y., Fukagawa, T., Kihara, A., Haraguchi, T., & Hiraoka, Y. (2023) · Journal of Cell Science · doi:10.1242/jcs.260923 · Cited by 6
In silico analysis of Hepatitis C virus (HCV) polyprotein domains and their comparison with other pathogens and allergens to gain insight on pathogenicity mechanisms
Patel, S. V. (2016) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2016.10.006 · Cited by 7
Enfermedad CLN8 congénita de lipofuscinosis neuronal ceroidea: un nuevo fenotipo
Pesaola, F. N., Kohan, R., Cismondi, I. A., Guelbert, N. B., Pons, P., Ramírez, A. M. O., & de Halac, I. N. (2019) · Revista de Neurología · doi:10.33588/rn.6804.2018217 · Cited by 7
Function of ceramide synthases on growth, ganoderic acid biosynthesis and sphingolipid homeostasis in Ganoderma lucidum
Lu, X., Xie, C., Wang, Y., Liu, Y., Han, J. D. J., Shi, L., Zhu, J. K., Yu, H., Ren, A., & Zhao, M. (2020) · Phytochemistry · doi:10.1016/j.phytochem.2020.112283 · Cited by 8
CLN8 Gene Compound Heterozygous Variants: A New Case and Protein Bioinformatics Analyses
Sharkia, R. A., Zalan, A. A., Zahalka, H., Kessel, A., Asaly, A., Al-Shareef, W., & Mahajnah, M. M. (2022) · Genes · doi:10.3390/genes13081393 · Cited by 6
“It contains the TLC (TRAM-LAG1-CLN8) domain, involved in the homeostasis of brain lipids: synthesis, sensing, transport, and metabolism [15].”
Background
The Neuronal Ceroid Lipofuscinoses-Linked Loss of Function CLN5 and CLN8 Variants Disrupt Normal Lysosomal Function
Parvin, S., Rezazadeh, M., Hosseinzadeh, H., Moradi, M., Shiva, S., & Gharesouran, J. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-019-08529-7 · Cited by 6
CERS6 promotes esophageal squamous cell carcinoma proliferation by increasing the stability of RPN1
Chen, W., Zhai, Y., Yang, X., Zhang, W., Gao, D., Zhao, X., Zhao, N., Zhang, Y., Yuan, Q., Zhao, Z., et al. (2025) · Cell Death Discovery · doi:10.1038/s41420-025-02727-y · Cited by 5
“Moreover, targeting CERS6 inhibited the growth of ESCC through the RPN1-IRE1-XBP1 signaling pathway, indicating that CERS6 may be a promising therapeutic target for ESCC.”
The Role of Longevity Assurance Homolog 2/Ceramide Synthase 2 in Bladder Cancer
Garcia‐Vallicrosa, C., Falcón‐Pérez, J. M., & Royo, F. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115668 · Cited by 6
“The latter is a translocation domain [27] essential for CERS activity, and it exhibits structures required for catalysis and substrate binding [28,29].”
Background
Molecular and biochemical components associated with chilling tolerance in tomato: comparison of different developmental stages
Camalle, M. D., Levin, E., David, S., Faigenboim, A., Foolad, M. R., & Lers, A. (2024) · Molecular Horticulture · doi:10.1186/s43897-024-00108-0 · Cited by 5
“…expasy. org ); the TLC domain is found in a family of membrane-associated proteins predicted to contain five transmembrane α helices (Si et al. 2019; Winter and Ponting 2002); although the role of the TLC domain is unknown, possible functions include involvement in lipid metabolism, sensing, or…”
Background
Identification of residues critical for topology inversion of the transmembrane protein TM4SF20 through regulated alternative translocation
Wang, J.-C., Kinch, L. N., Denard, B., Lee, C.-E., Gharehdaghi, E. E., Grishin, N., & Ye, J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007681 · Cited by 7
“TRAM2 contains a TLC domain postulated to bind ceramide or related sphingolipids (18).”
Background
Membrane topology of yeast alkaline ceramidase YPC1
Ramachandra, N., & Conzelmann, A. (2013) · Biochemical Journal · doi:10.1042/bj20130085 · Cited by 5
The revelation of selective sphingolipid pathway inhibition mechanism on fumonisin toxin binding to ceramide synthases in susceptible organisms and survival mechanism in resistant species
Sharma, S., Ahmed, M., & Akhter, Y. (2018) · Biochimie · doi:10.1016/j.biochi.2018.03.014 · Cited by 5
Functions of Ceramide Synthase Paralogs YPR114w and YJR116w of Saccharomyces cerevisiae
Mallela, S. K., Almeida, R., Ejsing, C. S., & Conzelmann, A. (2016) · PLoS ONE · doi:10.1371/journal.pone.0145831 · Cited by 4
“YJR116w and YPR114w also retain only the first His of a conserved His-His motif present in all ascertained ceramide synthases [4].”
Background
The Neuronal Ceroid Lipofuscinoses
Mole, S. (2024) · Oxford University Press eBooks · doi:10.1093/med/9780197549469.003.0050 · Cited by 3
An anomalous abundance of tryptophan residues in ceramide synthases based on analysis of all membrane proteins in the Swiss-Prot database
Mestre, B., Zelnik, I. D., Izrailov, S., Dingjan, T., Lvovsky, G., Fidel, L., Ben‐Dor, S., & Futerman, A. H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.108053 · Cited by 3
“In contrast, human CerS1, which does not contain a Hox-like domain, exhibited a nearly symmetrical Trp distribution, likely due to the lack of a Trp cluster in its N-terminus; similarly, Tram1 [a TLC family member (12)] exhibited a uniform distribution of Trp residues (Fig.”
Inherited unbalanced translocation (4p16.3p15.32 duplication/8p23.3p23.2deletion) in the four generation pedigree with intellectual disability/developmental delay
Hao, D., Li, Y., Chen, L., Wang, X., Wang, M., & Yu, Y. (2021) · Molecular Cytogenetics · doi:10.1186/s13039-021-00552-3 · Cited by 3
“The autosomal recessive mutations of CLN8 gene were related to two abnormal phenotypes: progressive epilepsy and mental retardation (EPMR), also known as Northern epilepsy syndrome [23] and a variant late-infantile neuronal ceroid lipofuscinoses (v-LINCL), characterized by earlier onset, faster progression of the dise…”
Background
Ceramide Synthase
Pankova-Kholmyansky, I., & Futerman, A. H. (2006) · Springer eBooks · doi:10.1007/4-431-34200-1_3 · Cited by 3
The T Allele of rs8075977 in the 5′-Flanking Region of the PEDF Gene Is Associated with Reduced Risk of Coronary Artery Disease in Elderly Chinese Men
Ma, S., Guo, Y., Wang, S., Shi, J., Liu, J., Liu, J., & Zhu, P. (2017) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.241.297 · Cited by 3
Using local gene network approach to functionally link lifespan genes and nutrient metabolism modules in C. elegans
Tan, X., Xuan, D., Wang, J., & Zhang, Z. (2011) · International Conference on Remote Sensing, Environment and Transportation Engineering · doi:10.1109/rsete.2011.5966308 · Cited by 2
Effect of fumonisin B1 on the emergence, growth and ceramide synthase gene expression of cowpea (Vigna unguiculata (L.) Walp)
Kotze, R. G., Crampton, B. G., & Kritzinger, Q. (2016) · European Journal of Plant Pathology · doi:10.1007/s10658-016-1089-1 · Cited by 2
“Ceramide synthase is encoded by the longevity assurance gene or LAG1 gene family in the majority of eukaryotic organisms (Winter and Ponting 2002).”
Background
WITHDRAWN: Biochemistry of very-long-chain and long-chain ceramides in cystic fibrosis and other diseases: The importance of side chain
Garić, D., Sanctis, J. B. D., Shah, J., Dumut, D. C., & Radzioch, D. (2019) · Progress in Lipid Research · doi:10.1016/j.plipres.2019.100998 · Cited by 2
CLN5 : from mutation to defective protein and clinical phenotype
Holmberg, V. (2004) · Työväentutkimus Vuosikirja · Cited by 2
Novel Cln8 p.R24G mouse line replicates major clinical features of Northern epilepsyPreprint
Müller-Niva, J., Salo, A. M., Häkli, S., Gureviciene, I., Makiou, A., Koivisto, H., Elamaa, H. P., Miinalainen, I., Heikkinen, A., Eklund, L., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.02.690107 · Cited by 2
“Sequence homology links CLN8 to the large eukaryotic protein family of TLC-domain homologs (Winter & Ponting, 2002; Sheokand et al., 2025).”
Generation of a ceramide synthase 6 mouse lacking the DDRSDIE C-terminal motif
Kim, J., Pewzner‐Jung, Y., Joseph, T., Ben‐Dor, S., & Futerman, A. H. (2022) · PLoS ONE · doi:10.1371/journal.pone.0271675 · Cited by 1
Ceramides
de Avalos, S. V., Jones, J. A., & Hannun, Y. A. (2012) · Elsevier eBooks · doi:10.1533/9780857097934.135 · Cited by 1
Regulated Alternative Translocation: A Mechanism Regulating Transmembrane Proteins Through Topological Inversion
Ye, J. (2020) · Advances in experimental medicine and biology · doi:10.1007/5584_2020_585 · Cited by 1
Sphingolipid Disorders and the Neuronal Ceroid Lipofuscinoses or Batten Disease (Wolman Disease, Cholesteryl Ester Storage Disease, and Cerebrotendinous Xanthomatosis)
Boustany, R., Al-Shareef, I., & El-Haddad, S. (2013) · Elsevier eBooks · doi:10.1016/b978-0-12-383834-6.00109-9 · Cited by 1
Neuronal ceroid lipofuscinosis CLN8 - from gene to protein
Lonka, L. (2004) · Työväentutkimus Vuosikirja · Cited by 1
Espectro clínico-mutacional y estudios de correlación genotipo-fenotipo en la población española afectada de lipofuscinosis neuronal ceroidea
Poyato, P., & del Socorro, M. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) · Cited by 1
Neuronal Ceroid Lipofuscinoses: Many Players, and More to Come
Simonati, A., Cannelli, N., Pezzini, F., Aiello, C., Bianchi, M., Tessa, A., & Santorelli, F. M. (2009) · Future Neurology · doi:10.2217/fnl.09.38 · Cited by 1
Molecular Interactions of Neuronal Ceroid Lipofuscinosis Protein CLN3
Uusi-Rauva, K. (2012) · Työväentutkimus Vuosikirja · Cited by 1
DISSECTION OF THE GENETIC BACKGROUND OF CHILDHOOD ONSET PROGRESSIVE MYOCLONIC EPILEPSIES
Kousi, M. (2012) · Työväentutkimus Vuosikirja · Cited by 1
Rôle des sphingolipides dans la cancérogenèse : l'exemple de la maladie de Gaucher
Astudillo, L. M. (2016) · theses.fr (ABES) · doi:10.70675/fa7a5078z1170z48a0z81a7z05c9d8e7a135 · Cited by 1
Mass-spectrometric analysis of glycerophospholipid metabolism
Hermansson, M. (2012) · Työväentutkimus Vuosikirja
Myoclonic Epilepsy in Lysosomal Storage Disorders
Dardis, A., & Bembi, B. (2011) · InTech eBooks · doi:10.5772/19918
“Members of this family are involved in the biosynthesis, metabolisms, transport and sensing of lipids (Winter & Ponting, 2002).”
Molecular interactions underlying neuronal ceroid lipofuscinoses CLN1 and CLN5
Lyly, A. (2008) · Työväentutkimus Vuosikirja
Multiple drug resistance mechanisms in Imatinib resistant human chronic myeloid leukemia cells.
Baran, Y. (2006)
IDENTIFICATION OF TWO NOVEL HUMAN NEURONAL CEROID LIPOFUSCINOSIS GENES
Siintola, E. (2008) · Työväentutkimus Vuosikirja
Cathepsin D Deficiency : Molecular and Cellular Mechanisms of Neurodegeneration
Partanen, S. (2006) · Työväentutkimus Vuosikirja
Studies on the molecular pathogenesis of neuronal ceroid lipofuscinoses in the animal models of CLN8 and CLN10
Kuronen, M. (2012) · Työväentutkimus Vuosikirja
ANIMAL MODEL AND MOLECULAR INTERACTIONS OF CLN5
Tion, A. D. A. (2009)
Molecular Genetics of the Neuronal Ceroid Lipofuscinoses
Mole, S. (2014) · Encyclopedia of Life Sciences · doi:10.1002/9780470015902.a0024913
CELLULAR MECHANISMS OF NEURODEGENERATION
Partanen, S. (2006)
The role of ceramides in cigarette smoke-induced alveolar cell death
Kamocki, K. (2013) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1845
Inverting the Topology of a Transmembrane Protein by Regulating the Translocation of the First
Chen, Q., Denard, B. S., Lee, C., Han, S., Ye, J. S., & Ye, J. (2016)
Regulators of Membrane Fluidity
Busayavalasa, K. (2020) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Membrane Fluidity Regulation: From C. elegans to mammalian cells
Devkota, R. (2020) · Gothenburg University Publications Electronic Archive (Gothenburg University)
Rapid Divergence of Key Spermatogenesis Genes in nasuta-Subgroup of Drosophila
Chowdanayaka, R., & Ramachandra, N. B. (2021) · Journal of Molecular Evolution · doi:10.1007/s00239-021-10037-x
Animal model and molecular interactions of Cln5
von Schantz, C. (2009) · STM:n Hallinnonalan avoin julkaisuarkisto (Julkari)
Structural and functional dissection of a higher-order oligomerization interface in yeast ceramide synthase
FANG, Q., Yang, C., Yao, N., Xie, T., & Gong, X. (2026) · Nature Communications · doi:10.1038/s41467-026-71272-8
“All CerS catalytic subunits share a conserved TRAM-Lag-CLN8 (TLC) domain, which comprises six transmembrane helices (TMs) 44 .”
Criblage de petites molécules d'intérêt thérapeutique et recherche de leur mécanisme d'action
Rozié, A. (2020) · theses.fr (ABES) · doi:10.70675/cfe93a65zdad1z4f4fzb5e3z4c2daf8ea474
CerS2-mediated lipotoxicity and calcium signaling: a novel sequential mechanism of apoptosis in cancer
Narayan, S. (2026) · Biochemical Journal · doi:10.1042/bcj20260424
“The structural basis for the substrate specificity of CerS2 is located within its conserved catalytic TRAM-Lag1-CLN8 (TLC) domain, a hallmark of the CerS family [37,38].”

Authors: Winter, E., & Ponting, C. P.
Affiliations: University of Oxford (GB)
Corresponding author: Ponting, Chris P
ORCID: Winter, Eitan
Ponting, Chris P
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2002-08
Volume: 27
Issue: 8
Pages: 381-383
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/s0968-0004(02)02154-0
OpenAlex: W2016874659
Cited by: 181
References: 22
Citations by year: 2026: 2 · 2025: 3 · 2024: 8 · 2023: 4 · 2022: 4 · 2021: 9 · 2020: 9 · 2019: 8 · 2018: 8 · 2017: 4 · 2016: 11 · 2015: 4 · 2014: 5 · 2013: 10 · 2012: 16
FWCI: 0.55
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Sphingolipid Metabolism and Signaling
Health Sciences › Medicine › Genetics (clinical) › Lysosomal Storage Disorders Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Lipid metabolism and biosynthesis
Keywords: tram, CLN8, membrane-associated proteins, ceramide synthesis, lipid regulation, neuronal ceroid lipofuscinosis, protein families
MeSH terms: Amino Acid Sequence, Animals, Fungal Proteins, Humans, Membrane Glycoproteins, Membrane Proteins, Molecular Sequence Data, Mutation, Sequence Homology, Amino Acid, Protein Structure, Tertiary, Membrane Transport Proteins, Saccharomyces cerevisiae Proteins, Lipid Metabolism, Mice

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

TRAM, LAG1 and CLN8: members of a novel family of lipid-sensing domains?

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks