Discovery of new Longin and Roadblock domains that form platforms for small GTPases in Ragulator and TRAPP-II
Open accessAbstract
Guanine nucleotide exchange factors (GEFs) control the site and extent of GTPase activity. Longin domains (LDs) are found in many Rab-GEFs, including DENNs, MON1/CCZ1, BLOC-3 and the TRAPP complex. Other GEFs, including Ragulator, contain roadblock domains (RDs), the structure of which is closely related to LDs. Other GTPase regulators, including mglB, SRX and Rags, use LDs or RDs as platforms for GTPases. Here, we review the conserved relationship between GTPases and LD/RDs, showing how LD/RD dimers act as adaptable platforms for GTPases. To extend our knowledge of GEFs, we used a highly sensitive sequence alignment tool to predict the existence of new LD/RDs. We discovered two yeast Ragulator subunits, and also a new LD in TRAPPC10 that may explain the Rab11-GEF activity ascribed to TRAPP-II.
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The Ragulator-Rag complex serves as an extended interaction hub for the nutrient-sensing machinery, including the GAPs GATOR1 and FLCN-FNIP, peripheral lysosomal proteins such as v-ATPase and SLC38A9, and (m)TORC1.
“Given the notion that roadblock domains, like the structurally similar longin domains, are recurring architectures in GTPase-interacting proteins (Levine et al., 2013) the Ragulator-Rag complex serves as an extended interaction hub for the nutrient-sensing machinery, including the GAPs GATOR1 and FLCN-FNIP, peripheral lysosomal proteins such as v-ATPase and SLC38A9, and (m)TORC1.”
From Signal integration in the (m)TORC1 growth pathway (2018) · cites this paper as Levine et al., 2013
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“S6A), which is consistent with the bioinformatic analysis (24, 37).”
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SEA you later alli-GATOR – a dynamic regulator of the TORC1 stress response pathway
Dokudovskaya, S., & Rout, M. P. (2015) · Journal of Cell Science · doi:10.1242/jcs.168922 · Cited by 70 · see citing works
“Npr2 is a possible paralog of Npr3 (Kowalczyk et al., 2012a), and both proteins possess N-terminal longin domains, which are found in GEFs, although a GEF activity has not yet been demonstrated for these two proteins (Levine et al., 2013; Nookala et al., 2012; Zhang et al., 2012).”
BackgroundKiontke, S., Langemeyer, L., Kuhlee, A., Schuback, S., Raunser, S., Ungermann, C., & Kümmel, D. (2017) · Nature Communications · doi:10.1038/ncomms14034 · Cited by 73 · see citing works
Zhang, T., Wang, R., Wang, Z., Wang, X., Wang, F., & Ding, J. (2017) · Nature Communications · doi:10.1038/s41467-017-01567-4 · Cited by 72 · see citing works
Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases
Ishida, M., Oguchi, M. E., & Fukuda, M. (2016) · Cell Structure and Function · doi:10.1247/csf.16008 · Cited by 66 · see citing works
Pinar, M., Arst, H. N., Pantazopoulou, A., Tagua, V. G., Rı́os, V. D. L., Rodríguez‐Salarichs, J., Díaz, J. F., & Peñalva, M. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1419168112 · Cited by 65 · see citing works
“The sharp functional boundary between Ypt1 and Ypt31/Ypt32 is determined, at least in part, by an anticurrent cascade in which Gyp1, the GAP for Ypt1, is an effector of Ypt31/Ypt32, thus ensuring minimal overlap of the GTPases on the same membranes (11).”
BackgroundInfluentialUsing HHsearch to tackle proteins of unknown function: A pilot study with PH domains
Fidler, D. R., Murphy, S. E., Courtis, K., Antonoudiou, P., El‐Tohamy, R., Ient, J., & Levine, T. P. (2016) · Traffic · doi:10.1111/tra.12432 · Cited by 58 · see citing works
“HHsearch - more sensitive than PSI-BLAST Profile-profile tools such as HHsearch (Box 3) have previously detected many new domains((29-39)), so we asked if HHsearch can improve on PSI-BLAST for PH-like domains.”
BackgroundSelf-citationNumrich, J., Péli-Gulli, M.-P., Arlt, H., Sardu, A., Griffith, J. M., Levine, T. P., Engelbrecht-Vandré, S., Reggiori, F., Virgilio, C. D., & Ungermann, C. (2015) · Journal of Cell Science · doi:10.1242/jcs.164905 · Cited by 47 · see citing works
“We previously have characterized the palmitoylatedEgo1/Meh1protein on vacuoles (Hou et al., 2005), which is part of the EGO complex comprising Ego1, Ego3, and the two Rag GTPases Gtr1 and Gtr2 (Dubouloz et al., 2005; Levine et al., 2013; Zhang et al., 2012).”
BackgroundInfluentialSelf-citationFactors affecting yeast ethanol tolerance and fermentation efficiency
Vamvakas, S. M., & Kapolos, J. (2020) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-020-02881-8 · Cited by 56 · see citing works
Regulation of mTORC1 by the Rag GTPases
Lama-Sherpa, T. D., Jeong, M.-H., & Jewell, J. L. (2023) · Biochemical Society Transactions · doi:10.1042/bst20210038 · Cited by 53 · see citing works
Planar Cell Polarity Effector Proteins Inturned and Fuzzy Form a Rab23 GEF Complex
Gerondopoulos, A., Strutt, H. L., Stevenson, N. L., Sobajima, T., Levine, T. P., Stephens, D. J., Strutt, D. I., & Barr, F. A. (2019) · Current Biology · doi:10.1016/j.cub.2019.07.090 · Cited by 47 · see citing works
“ED C Intu: Fuz: - - + + IP: FLAG-IntuInput + +- - 46 100 46 FLAG-Intu Myc-Fuz Actin - - + + + +- - kDa F A Fuz B 942 265 452 652 1 183 Intu 146 289 7950 303 477 792 PDZ LD14181 LD1 LD2 LD2 LD3WW 1 LD3 LD1 LD2 LD3 155 297 421 555Mon1 177 491 7001 LD1 LD2 1 LD1 LD2 LD3 183 372 482Ccz1 LD3Hps1 166 7081 LD1Hps4 LD3 600265…”
InfluentialSelf-citationLongin and GAF Domains: Structural Evolution and Adaptation to the Subcellular Trafficking Machinery
Franceschi, N. D., Wild, K., Schlacht, A., Dacks, J. B., Sinning, I., & Filippini, F. (2013) · Traffic · doi:10.1111/tra.12124 · Cited by 46 · see citing works
Cryo‐EM structure of metazoan TRAPPIII, the multi‐subunit complex that activates the GTPase Rab1
Galindo, A., Planelles-Herrero, V. J., Degliesposti, G., & Munro, S. (2021) · The EMBO Journal · doi:10.15252/embj.2020107608 · Cited by 39 · see citing works
“…studies of the individual core subunits and their subcomplexes have revealed that the centre of the core comprises two longin domain proteins, TRAPPC1 and TRAPPC4, consistent with longin domains being present in several other Rab GEFs (Kim et al, 2006; Cai et al, 2008; Levine et al, 2013).”
Nutrient Signaling and Lysosome Positioning Crosstalk Through a Multifunctional Protein, Folliculin
Garrido, N. D. M., & Aylett, C. H. S. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00108 · Cited by 33 · see citing works
C9orf72’s Interaction with Rab GTPases—Modulation of Membrane Traffic and Autophagy
Tang, B. L. (2016) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2016.00228 · Cited by 36 · see citing works
Morris, C. S., Foster, O. K., Handa, S., Peloza, K., Voss, L. A., Somhegyi, H., Jian, Y., Vo, M. V., Harp, M., Rambo, F. M., et al. (2018) · PLoS Genetics · doi:10.1371/journal.pgen.1007772 · Cited by 36 · see citing works
Amino acid and small GTPase regulation of mTORC1
Nguyen, T. P., Frank, A., & Jewell, J. L. (2017) · Cellular Logistics · doi:10.1080/21592799.2017.1378794 · Cited by 30 · see citing works
“Consistently, Ego2 and Ego3 contain roadblock domain-like folds which serve as the interaction surface for the Gtr1-Gtr2 dimer, reinforcing the structural and functional similarities between Ragulator and EGOC.(40) Although there is significant functional and structural similarity between the Rag and Gtr complexes as…”
BackgroundInfluentialTumor suppressor NPRL2 induces ROS production and DNA damage response
Ma, Y.-X., Silveri, L., LaCava, J., & Dokudovskaya, S. (2017) · Scientific Reports · doi:10.1038/s41598-017-15497-0 · Cited by 22 · see citing works
Kandachar, V., Tam, B. M., Moritz, O. L., & Deretic, D. (2018) · Journal of Cell Science · doi:10.1242/jcs.222034 · Cited by 33 · see citing works
“Rab GTPases as coordinators of vesicle traffic.”
BackgroundInfluentialVacuolin-1 inhibits endosomal trafficking and metastasis via CapZβ
Ye, Z., Wang, D., Lü, Y., He, Y., Yu, J., Wei, W., Chen, C., Wang, R. Y., Zhang, L. N., Zhang, L., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01662-3 · Cited by 32 · see citing works
Wei, Y., Reveal, B., Cai, W., & Lilly, M. A. (2016) · G3 Genes|Genomes|Genetics · doi:10.1534/g3.116.035337 · Cited by 31 · see citing works
“Both Nprl2 and Nprl3 contain a C-terminal Longin domain, which is often found in proteins that regulate membrane traf fi cking (Levine et al. 2013), followed by two or three N-terminal helix-turn-helix domains (Zhang et al. 2012; Levine et al. 2013).”
Diab, R., Pilotto, F., & Saxena, S. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2023.1086895 · Cited by 31 · see citing works
Amino acids stimulate the endosome-to-Golgi trafficking through Ragulator and small GTPase Arl5
Shi, M., Chen, B., Mahajan, D., Boh, B. K., Zhou, Y., Dutta, B., Tie, H. C., Sze, S. K., Wu, G., & Lü, L. (2018) · Nature Communications · doi:10.1038/s41467-018-07444-y · Cited by 30 · see citing works
Lst4, the yeast Fnip1/2 orthologue, is a DENN-family protein
Pacitto, A., Ascher, D. B., Wong, L. H., Blaszczyk, B. K., Nookala, R. K., Zhang, N., Dokudovskaya, S., Levine, T. P., & Blundell, T. L. (2015) · Open Biology · doi:10.1098/rsob.150174 · Cited by 28 · see citing works
“While the core members are reasonably well conserved at the sequence level, the wider family is much more divergent and could only be detected by a more sensitive fold-recognition approach [18,19].”
BackgroundSelf-citationDelahaye, J. L., Foster, O. K., Vine, A., Saxton, D. S., Curtin, T. P., Somhegyi, H., Salesky, R., & Hermann, G. J. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-09-0521 · Cited by 27 · see citing works
“Molecular Biology of the Cell domain–containing proteins (Collins et al., 2002; Kim et al., 2006; Yu et al., 2009; Marat et al., 2011; Levine et al., 2013; De Franceschi et al., 2014).”
BackgroundBaranwal, J., Lhospice, S., Kanade, M., Chakraborty, S., Gade, P., Harne, S., Herrou, J., Mignot, T., & Gayathri, P. (2019) · PLoS Biology · doi:10.1371/journal.pbio.3000459 · Cited by 26 · see citing works
Jenkins, M. L., Harris, N. J., Dalwadi, U., Fleming, K. D., Ziemianowicz, D. S., Rafiei, A., Martin, E. M., Schriemer, D. C., Yip, C. K., & Burke, J. E. (2020) · Communications Biology · doi:10.1038/s42003-020-01459-2 · Cited by 26 · see citing works
Structure of the Mon1-Ccz1 complex reveals molecular basis of membrane binding for Rab7 activation
Klink, B. U., Herrmann, E., Antoni, C., Langemeyer, L., Kiontke, S., Gatsogiannis, C., Ungermann, C., Raunser, S., & Kümmel, D. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2121494119 · Cited by 26 · see citing works
“While the LD1s and LD2s are classical Longin-type and roadblock domains, respectively (24), LD3 is a lamtor-type domain in both Mon1 and Ccz1 (Fig.”
BackgroundThe TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11
Galindo, A., & Munro, S. (2022) · FEBS Letters · doi:10.1002/1873-3468.14553 · Cited by 23 · see citing works
The ins and outs of the Arf4-based ciliary membrane-targeting complex
Deretic, D., Lorentzen, E., & Fresquez, T. (2019) · Small GTPases · doi:10.1080/21541248.2019.1616355 · Cited by 25 · see citing works
Proposed Role for KaiC-Like ATPases as Major Signal Transduction Hubs in Archaea
Makarova, K. S., Galperin, M. Y., & Koonin, E. V. (2017) · mBio · doi:10.1128/mbio.01959-17 · Cited by 26 · see citing works
“4), and with Ras-like GTPases, either directly through the interaction with Srp102/FtsY or through Roadblock family proteins as described for both bacteria and eukaryotes (58, 59).”
BackgroundSpatiotemporal regulation of switching front–rear cell polarity
Carreira, L. A. M., Szadkowski, D., Müller, F., & Søgaard‐Andersen, L. (2022) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2022.102076 · Cited by 20 · see citing works
Tran, L. T., Akıl, C., Senju, Y., & Robinson, R. C. (2024) · Communications Biology · doi:10.1038/s42003-024-05888-1 · Cited by 21 · see citing works
“GEFs are structurally diverse, and can form large complexes which often contain subunits of the roadblock (RB)/longin families of proteins 5 .”
InfluentialVetter, M., Wang, J., Lorentzen, E., & Deretic, D. (2015) · Small GTPases · doi:10.1080/21541248.2015.1091539 · Cited by 18 · see citing works
Loissell-Baltazar, Y. A., & Dokudovskaya, S. (2021) · Cells · doi:10.3390/cells10102689 · Cited by 17 · see citing works
“RAG GTPases regulate the recruitment of TSC to the lysosome and its ability to interact with and inhibit RHEB in response to amino acid starvation, growth factors removal and to other stresses that inhibit mTORC1 [73–75].”
BackgroundInfluentialUnorthodox regulation of the MglA Ras‐like GTPase controlling polarity in Myxococcus xanthus
Dinet, C., & Mignot, T. (2022) · FEBS Letters · doi:10.1002/1873-3468.14565 · Cited by 13 · see citing works
Hexa-Longin domain scaffolds for inter-Rab signalling
Sánchez‐Pulido, L., & Ponting, C. P. (2019) · Bioinformatics · doi:10.1093/bioinformatics/btz739 · Cited by 13 · see citing works
Carreira, L. A. M., Szadkowski, D., Lometto, S., Hochberg, G. K. A., & Søgaard‐Andersen, L. (2023) · Nature Communications · doi:10.1038/s41467-023-39773-y · Cited by 13 · see citing works
“The roadblock domain protein family is ancient, abundantly present in all domains of life, and often involved in regulating GTPase activity 37,46 – 48 .”
Function of the Mon1-Ccz1 complex on endosomes
Cabrera, M., Engelbrecht-Vandré, S., & Ungermann, C. (2014) · Small GTPases · doi:10.4161/sgtp.29040 · Cited by 13 · see citing works
“Sequence analysis of Mon1 and Ccz1 proteins has revealed the presence of longin folds, which are also found in the TRAPP subunits Bet5 and Trs23.(16,17) The prediction of these domains in Mon1/Ccz1 suggests a similar GEF mechanism for this complex.”
BackgroundSignal integration in the (m)TORC1 growth pathway
Ramlaul, K., & Aylett, C. H. S. (2018) · Frontiers in Biology · doi:10.1007/s11515-018-1501-7 · Cited by 12 · see citing works
The progress inC9orf72research: ALS/FTD pathogenesis, functions and structure
Jiang, L., Zhang, T., Lu, K., & Qi, S. (2021) · Small GTPases · doi:10.1080/21541248.2021.1892443 · Cited by 12 · see citing works
Encoding Allostery in mTOR Signaling: The Structure of the Rag GTPase/Ragulator Complex
Cherfils, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.027 · Cited by 12 · see citing works
C7orf59/LAMTOR4 phosphorylation and structural flexibility modulate Ragulator assembly
Rasheed, N., Lima, T. B., Mercaldi, G. F., Nascimento, A. F. Z., Silva, A. L. S., Righetto, G. L., Bar‐Peled, L., Shen, K., Sabatini, D. M., Gozzo, F. C., et al. (2019) · FEBS Open Bio · doi:10.1002/2211-5463.12700 · Cited by 12 · see citing works
TOR Signaling in Budding Yeast
Inoue, Y., & Nomura, W. (2018) · InTech eBooks · doi:10.5772/intechopen.70784 · Cited by 10 · see citing works
“Ego2 and Ego3 bind to vacuolar membrane-anchored Ego1 [35].”
BackgroundSaikat, A. S. M. (2023) · Genomics & Informatics · doi:10.5808/gi.23001 · Cited by 10 · see citing works
Kapoor, S., Kodesia, A., Kalidas, N., Ashish, & Thakur, K. G. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100308 · Cited by 9 · see citing works
“Based on the multiple sequence alignment (MSA) and predicted secondary structure assignments, MglC has been predicted to be a member of RLC7 family proteins (30).”
BackgroundSaikat, A. S. M., Das, R. C., & Das, M. C. (2022) · International Electronic Conference on Synthetic Organic Chemistry (ECSOC) · doi:10.3390/ecsoc-26-13530 · Cited by 8 · see citing works
“Determination and Validation of the Three-Dimensional Protein Structure The three-dimensional structure of the selected protein was anticipated by using the Modeller [24] with the HHpred interface [25,26].”
Methodkm23‐1/DYNLRB1 regulation of MEK/ERK signaling and R‐Ras in invasive human colorectal cancer cells
Raza, A., Pandey, M. S., Jin, Q., & Mulder, K. M. (2019) · Cell Biology International · doi:10.1002/cbin.11215 · Cited by 8 · see citing works
“Thus, the km23‐1‐Ras‐binding function for regulation of cell motility appears to have been conserved throughout evolution (Koonin and Aravind, 2000; Levine et al., 2013; De Franceschi et al., 2014).”
Yong, X., Jia, G., Yang, Q., Zhou, C., Zhang, S., Deng, H., Billadeau, D. D., Su, Z., & Jia, D. (2025) · Nature Communications · doi:10.1038/s41467-025-58235-1 · Cited by 7 · see citing works
“The LD1, LD2, and LD3 of HPS1 andHPS4adoptacanonicallonginfold,aroadblocklongin-likefold,and alamtorlongin-likefold,respectively 25,26 (Figs.1d,e, 2a).”
Bertuzzi, M., Tang, D. T. P., Calligaris, R., Vlachouli, C., Finaurini, S., Sanges, R., Goldwurm, S., Catalan, M., Antonutti, L., Manganotti, P., et al. (2020) · Human Mutation · doi:10.1002/humu.23974 · Cited by 6 · see citing works
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Amyotrophic Lateral Sclerosis: Focus on Cytoplasmic Trafficking and Proteostasis
Shrilaxmi, M. S., Banerjee, S., D’Mello, S. R., & Dastidar, S. G. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04831-7 · Cited by 6 · see citing works
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Principles of Protein Structure and Function
Smetana, J. H. C., & Misra, G. (2017) · Springer eBooks · doi:10.1007/978-981-10-4968-2_1 · Cited by 5 · see citing works
Structures and Functions of the Human GATOR1 Complex
Ivanova, I., & Shen, K. (2024) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-58843-3_12 · Cited by 4 · see citing works
Chakraborty, S., Kanade, M., & Gayathri, P. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107197 · Cited by 4 · see citing works
Structural basis of pseudoGTPase-mediated protein-protein interactions
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Cell polarity control by an unconventional G-protein complex in bacteria
Dinet, C., Sebban‐Kreuzer, C., Byrne, D., Lhospice, S., Herrou, J., Durbesson, F., Vincentelli, R., Calvez, V., Sturgis, J. N., Michelot, A., et al. (2026) · Nature Communications · doi:10.1038/s41467-026-74081-1 · Cited by 3 · see citing works
“They are typically incorporated into complex molecular scaffolds, where they primarily function as guanine nucleotide exchange factors (GEFs) but occasionally act as GTPase-activating proteins (GAPs) through allosteric regulation or with the help of additional regulatory components 41,52,54,55 .”
Eukaryote‐Wide Distribution of a Family of Longin Domain‐Containing GAP Complexes for Small GTPases
Vanclová, A. M. G. N., Jackson, C. L., & Dacks, J. B. (2025) · Traffic · doi:10.1111/tra.70016 · Cited by 1 · see citing works
“…generally highly conserved, short, single domain proteins, their GEFs and GAPs usually contain multiple Traffic, 2025 domains in addition to the catalytic domain (e.g., PH, SH3, C2, coiled-coil, BAR, ankyrin-repeat, WD40 or RUN [4, 10, 12]) and are much more varied in their size and architecture.”
KaiC-like ATPases as Signal Transduction Hubs in Archaea
Makarova, K. S., & Koonin, E. V. (2017) · Springer eBooks · doi:10.1007/978-3-319-65536-9_11 · Cited by 2 · see citing works
Rab GEFs and GAPs: The Enigma Variations
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“Bet3 and Bet5 are both longin domain proteins and form a dimeric platform for Rab binding (Kinch and Grishin 2006; Levine et al. 2013) (Fig.”
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Evolutionary conservation of Rag GTPase regulation
Panchaud, N., Gulli, M., & VIRGILIO, C. D. (2013)
Rolle der -COP-Untereinheit im frühen sekretorischen Pfad
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Characterization of the role of TRAPPC2/Trs20p-related and associated proteins in membrane traffic
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Biochemical characterization of mTORC1 regulation by glutamine metabolism
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The role of GATOR1 complex, upstream regulator of mTORC1 pathway, in mitochondrial function
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Cryo-EM structure of the WDR11-FAM91A1-C17orf75 complex involved in retrograde trafficking
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- Authors
- Levine, T. P., Daniels, R. D., Wong, L. H., Gatta, A. T., Gerondopoulos, A., & Barr, F. A.
- Affiliations
- University College London (GB)
- University of Oxford (GB)
- Venue
- Small GTPases
- Publisher
- Informa UK Limited
- Published
- 2013-04
- Volume
- 4
- Issue
- 2
- Pages
- 62-69
- ISSN
- 2154-1248 (ISSN-L)
- 2154-1256
- PMC
- PMC3747258
- OpenAlex
- W2092636253
- Cited by
- 93
- References
- 54
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 3 · 2023: 5 · 2022: 8 · 2021: 6 · 2020: 8 · 2019: 9 · 2018: 6 · 2017: 12 · 2016: 9 · 2015: 8 · 2014: 8 · 2013: 5
- FWCI
- 1.15
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Small GTPases (publishedVersion, cc-by-nc)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Wellcome Trust (097769/Z/11/Z, 097769)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- longin domain, guanine nucleotide exchange factor, Rab11, Rab GTPases, denn, yeast
- MeSH terms
- Amino Acid Sequence, Animals, Humans, Models, Molecular, Molecular Sequence Data, Yeasts, Protein Structure, Tertiary, Monomeric GTP-Binding Proteins, Guanine Nucleotide Exchange Factors
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