RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity
Open accessAbstract
We report that during cortical development in the mouse embryo, reversion-inducing cysteine-rich protein with Kazal motifs (RECK) critically regulates Notch signaling by antagonizing the ectodomain shedding of Notch ligands, which is mediated by a disintegrin and metalloproteinase domain 10 (ADAM10). In the embryonic brain, RECK is specifically expressed in Nestin-positive neural precursor cells (NPCs). Reck-deficient NPCs undergo precocious differentiation that is associated with downregulated Nestin expression, impaired Notch signaling and defective self-renewal. These phenotypes were substantially rescued either by enhancing Notch signaling or by suppressing endogenous ADAM10 activity. Consequently, we found that RECK regulates the ectodomain shedding of Notch ligands by directly inhibiting the proteolytic activity of ADAM10. This mechanism appeared to be essential for Notch ligands to properly induce Notch signaling in neighboring cells. These findings indicate that RECK is a physiological inhibitor of ADAM10, an upstream regulator of Notch signaling and a critical modulator of brain development.
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“ADAM10 is a Notch1 shedding enzyme which can be inhibited by RECK in neuronal progenitor cells (Muraguchi et al., 2007).”
BackgroundMolecular Regulation of Sprouting Angiogenesis
Duran, C. L., Howell, D. W., Dave, J. M., Smith, R. L., Torrie, M. E., Essner, J. J., & Bayless, K. J. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160048 · Cited by 76 · see citing works
Berezin, V., Walmod, P. S., Filippov, M. A., & Dityatev, A. E. (2014) · Progress in brain research · doi:10.1016/b978-0-444-63486-3.00015-3 · Cited by 62 · see citing works
Omura, A., Matsuzaki, T., Mio, K., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806212200 · Cited by 65 · see citing works
Self-citationADAMs family and relatives in cardiovascular physiology and pathology
Zhang, P., Shen, M., Fernández-Patrón, C., & Kassiri, Z. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.10.031 · Cited by 63 · see citing works
The metalloproteinase inhibitor Reck is essential for zebrafish DRG development
Prendergast, A. E., Linbo, T. H., Swarts, T., Ungos, J. M., McGraw, H. F., Krispin, S., Weinstein, B. M., & Raible, D. W. (2012) · Development · doi:10.1242/dev.072439 · Cited by 63 · see citing works
“…has demonstrated that Reck is a GPI-linked protein that inhibits metalloproteinases in cis, blocking activity in the cell in which it is expressed (Muraguchi et al., 2007). reck is expressed in both neural crest and the environment through which it migrates, including vascular precursors that…”
BackgroundInfluentialReck enables cerebrovascular development by promoting canonical Wnt signaling
Ulrich, F., Carretero-Ortega, J., Menéndez, J., Narvaez, C., Sun, B. L., Lancaster, E. E., Pershad, V., Trzaska, S., Véliz, E., Kamei, M., et al. (2015) · Development · doi:10.1242/dev.123059 · Cited by 63 · see citing works
“Reck modulates the development of forelimbs, dorsal root ganglia neurons (DRG), brain (Muraguchi et al., 2007; Park et al., 2013; Prendergast et al., 2012; Yamamoto et al., 2012) and vasculature.”
The role of Delta-like 1 shedding in muscle cell self-renewal and differentiation
Sun, D., Li, H. Z., & Żółkiewska, A. (2008) · Journal of Cell Science · doi:10.1242/jcs.035493 · Cited by 62 · see citing works
“, 2005) and in cortical neurogenesis in mice (Muraguchi et al., 2007).”
BackgroundMT1‐MMP cleaves Dll1 to negatively regulate Notch signalling to maintain normal B‐cell development
Jin, G., Zhang, F., Chan, K. M., Wong, H. L. X., Liu, B., Cheah, K. S. E., Liu, X., Mauch, C., Liu, D., & Zhou, Z. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.136 · Cited by 59 · see citing works
“In mammalian bone marrow, fibroblast-like stromal cells contribute critically to the development of haematopoietic cells, including stem cell maintenance and lineage cell development, by direct contact or release of cytokines (Nagasawa, 2006).”
BackgroundResultEndogenous and synthetic MMP inhibitors in CNS physiopathology.
Baranger, K., Rivera, S., Liechti, F., Grandgirard, D., Bigas, J., Seco, J., Tarragó, T., Leib, S., & Khrestchatisky, M. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00014-1 · Cited by 43 · see citing works
Morioka, Y., Monypenny, J., Matsuzaki, T., et al. (2009) · Oncogene · doi:10.1038/onc.2008.486 · Cited by 52 · see citing works
Self-citationInflammation without neuronal death triggers striatal neurogenesis comparable to stroke
Chapman, K. Z., Ge, R., Monni, E., Tatarishvili, J., Ahlenius, H., Arvidsson, A., Ekdahl, C. T., Lindvall, O., & Kokaia, Z. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.08.013 · Cited by 51 · see citing works
“Interestingly, our microarray analysis found that Timp1, a factor identified as inhibiting the Notch shedding enzyme ADAM10 (Rapti et al., 2008; Muraguchi et al., 2007; Amour et al., 2000), was upregulated in microglia sorted from the striatum of LPS-injected and MCAO-subjected rats (Table 4).”
BackgroundRosenbaum, D., & Säftig, P. (2023) · FEBS Journal · doi:10.1111/febs.16870 · Cited by 53 · see citing works
“The transmembrane protein reversion-inducing cysteine-rich protein with kazal motifs (RECK) also exerts a potent inhibitory effect on ADAM10 through a to date poorly characterized mechanism [168,169].”
BackgroundChandana, E. P. S., Maeda, Y., Ueda, A., Kiyonari, H., Oshima, N., Yamamoto, M., Kondo, S., Oh, J., Takahashi, R., Yoshida, Y., et al. (2010) · BMC Developmental Biology · doi:10.1186/1471-213x-10-84 · Cited by 48 · see citing works
“RECK has also been implicated in the regulation of several developmental processes, including embryonic angiogenesis, myogenesis, chondrogenesis, neurogenesis, and maturation of neuro-muscular junctions [15,19-22].”
BackgroundSelf-citationMcRobb, L. S., McKay, M. J., Gamble, J. R., Grace, M., Moutrie, V., Santos, E. D., Lee, V. S., Zhao, Z., Molloy, M. P., & Stoodley, M. A. (2017) · Aging · doi:10.18632/aging.101225 · Cited by 47 · see citing works
“Both ADAM10 and gamma-secretase activity appear to post-translationally regulate NEST expression and subcellular localization [64, 66].”
BackgroundFolate, Homocysteine and the Cardiac Neural Crest
Rosenquist, T. H. (2013) · Developmental Dynamics · doi:10.1002/dvdy.23922 · Cited by 46 · see citing works
“…Notch into the raft as well as the timing of its proteolytic cleavage are key events in early development of the cranial portion of the neural tube (Muraguchi et al., 2007; Watanabe et al., 2009) and, given the role of Notch for both the neural tube and the neural crest (Niessen and Karsan, 2008;…”
BackgroundRECK‐mediated inhibition of glioma migration and invasion
Corrêa, T. C. S., Massaro, R. R., Brohem, C. A., Taboga, S. R., Lamers, M. L., dos Santos, M. F., & Maria–Engler, S. S. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22472 · Cited by 46 · see citing works
“Other functions have recently been attributed to differential expression of RECK in processes such as angiogenesis [Oh et al., 2001; Muraguchi et al., 2007], chondrogenesis [Kondo et al.”
BackgroundResultInfluentialRegulation of the α-secretase ADAM10 at transcriptional, translational and post-translational levels
Vincent, B. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.03.020 · Cited by 45 · see citing works
Wang, R., Ye, X., Bhattacharya, R., Boulbés, D. R., Fan, F., Xia, L., & Ellis, L. M. (2016) · Stem Cells Translational Medicine · doi:10.5966/sctm.2015-0168 · Cited by 44 · see citing works
Donovan, L. E., Dammer, E. B., Duong, D. M., Hanfelt, J., Levey, A. I., Seyfried, N. T., & Lah, J. J. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt186 · Cited by 43 · see citing works
“Muraguchi T, Takegami Y, Ohtsuka T, Kitajima S, Chandana EPS, Omura A, Miki T, Takahashi R, Matsumoto N, Ludwig A, Noda M, Takahashi C: RECK modulates Notch signaling during cortical neurogenesis by regulating ADAM10 activity.”
BackgroundMummidi, S., Das, N. A., Carpenter, A. J., Yoshida, T., Manjunath, Y., Mostany, R., Izadpanah, R., Higashi, Y., Sukhanov, S., Noda, M., et al. (2019) · Journal of Cellular Physiology · doi:10.1002/jcp.28792 · Cited by 42 · see citing works
“Importantly, RECK directly inhibits ADAM10 proteolytic activity (Muraguchi et al., 2007).”
Self-citationSiddesha, J. M., Valente, A. J., Sakamuri, S. S. V. P., et al. (2013) · Journal of Cellular Physiology · doi:10.1002/jcp.24511 · Cited by 39 · see citing works
“In addition, RECK has also been shown to inhibit ADAM10 (a disintegrin and metalloproteinase domain 10; Muraguchi et al., 2007) and ADAM17 (Hong et al., 2013), members of the metzincin subgroup of zinc proteases, that play a role in cytokine release, growth factor activation, and cell-cell, and…”
BackgroundSelf-citationGDE2-RECK controls ADAM10 α-secretase–mediated cleavage of amyloid precursor protein
Nakamura, M., Li, Y., Choi, B.-R., Matas-Rico, E., Troncoso, J., Takahashi, C., & Sockanathan, S. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe6178 · Cited by 38 · see citing works
“Gde2−/− mice, APP/PS1 mice, Reck+/− mice, and RosaCreER;Gde2lox/− mice were generated, genotyped, and maintained as previously described (21, 32, 55).”
BackgroundMethodSelf-citationKuz and TACE can activate Notch independent of ligand
Delwig, A., & Rand, M. D. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8127-x · Cited by 36 · see citing works
“and MDR, unpublished observation and [41]) which may be the underlying reason that ADAM10 shows activity in regulating the Delta ligand in a mouse model [34].”
Involvement of the SKP2–p27KIP1 pathway in suppression of cancer cell proliferation by RECK
Yoshida, Y., Ninomiya, K., Hamada, H., et al. (2011) · Oncogene · doi:10.1038/onc.2011.570 · Cited by 32 · see citing works
“Global Reck-deficient mice, however, die too early (Oh et al., 2001; Muraguchi et al., 2007) and provide no direct answers to this question; the embryonic lethality of Reck-deficient mice probably reflects the multiplicity of RECK targets/effectors that are essential for embryogenesis.”
InfluentialSelf-citationKitajima, S., Miki, T., Takegami, Y., Kido, Y., Noda, M., Hara, E., Shamma, A., & Takahashi, C. (2010) · Oncogene · doi:10.1038/onc.2010.448 · Cited by 32 · see citing works
“RECK appeared to bind directly to ADAM10 and allosterically inhibit its proteolytic activity (Muraguchi et al., 2007).”
BackgroundMethodResultInfluentialSelf-citationMasuda, T., Fukuda, A., Yamakawa, G., Omatsu, M., Namikawa, M., Sono, M., Fukunaga, Y., Nagao, M., Araki, O., Yoshikawa, T., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci161847 · Cited by 16 · see citing works
“5 and show increased gelatinase activity in the tissue, decreased tissue integrity, and abnormalities in vascular and neural development (8, 12, 13).”
BackgroundSelf-citationNKX2.2 Suppresses Self-Renewal of Glioma-Initiating Cells
Muraguchi, T., Tanaka, S., Yamada, D., Tamase, A., Nakada, M., Nakamura, H., Hoshii, T., Ooshio, T., Tadokoro, Y., Naka, K., et al. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2304 · Cited by 29 · see citing works
“To assay TNS numbers, dissociated cells (2 10(3) cells/200 mL) were seeded into 96-well plates and cultured for 7 days in medium containing 20 ng/mL fibroblast growth factor-2 (FGF-2; Peprotech) and 20 ng/mL epidermal growth factor (EGF; Peprotech) as described (18).”
MethodInfluentialSelf-citationThe emergence of ADAM10 as a regulator of lymphocyte development and autoimmunity
Gibb, D. R., Saleem, S. J., Chaimowitz, N. S., Mathews, J. A., & Conrad, D. H. (2011) · Molecular Immunology · doi:10.1016/j.molimm.2010.12.005 · Cited by 31 · see citing works
The β1-Integrin–Dependent Function of RECK in Physiologic and Tumor Angiogenesis
Miki, T., Shamma, A., Kitajima, S., Takegami, Y., Noda, M., Nakashima, Y., Watanabe, K.-I., & Takahashi, C. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0351 · Cited by 30 · see citing works
“The specimens were fixed with 1% PFA, embedded in optimal cutting temperature compound, and stained as described previously (17).”
BackgroundMethodInfluentialSelf-citationThe interplay between microRNAs and Twist1 transcription factor: a systematic review
Khanbabaei, H., Teimoori, A., & Mohammadi, M. (2016) · Tumor Biology · doi:10.1007/s13277-016-4960-y · Cited by 30 · see citing works
The Wnt7's Tale: A story of an orphan who finds her tie to a famous family
Noda, M., Vallon, M., & Kuo, C. J. (2016) · Cancer Science · doi:10.1111/cas.12924 · Cited by 29 · see citing works
Self-citationModulation of Immune Responses by Platelet-Derived ADAM10
Maurer, S., Kopp, H., Salih, H. R., & Kropp, K. N. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00044 · Cited by 29 · see citing works
“Another physiological inhibitor of ADAM10 is the membrane-anchored RECK (153) and has been detected in the platelet membrane proteome (22).”
BackgroundRussell, J. J., Grisanti, L. A., Brown, S. M., Bailey, C. A., Bender, S. B., & Chandrasekar, B. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.109993 · Cited by 29 · see citing works
ADAM10-a “multitasker” in sepsis: focus on its posttranslational target
Liao, S., Lin, Y., Liu, L., Yang, S., Lin, Y., He, J., & Shao, Y. (2022) · Inflammation Research · doi:10.1007/s00011-022-01673-0 · Cited by 28 · see citing works
“Early investigation suggested that RECK expressed in the Central Nervous System (CNS) shut down Notch signaling by inhibiting its proteolysis via direct interaction with ADAM10 [136], which implies the protective function of RECK in sepsis by inhibiting ADAM10.”
BackgroundRECK overexpression decreases invasive potential in prostate cancer cells
Rabien, A., Erguen, B., Erbersdobler, A., et al. (2011) · The Prostate · doi:10.1002/pros.21498 · Cited by 27 · see citing works
“CD13/aminopeptidase N and a disintegrin and metalloproteinase 10 (ADAM10) are further RECK targets [2,4].”
BackgroundIrreversible modifications of receptor tyrosine kinases
Kreitman, M., Noronha, A., & Yarden, Y. (2018) · FEBS Letters · doi:10.1002/1873-3468.13095 · Cited by 26 · see citing works
Critical roles for murine Reck in the regulation of vascular patterning and stabilization
de Almeida, G. M., Yamamoto, M., Morioka, Y., et al. (2015) · Scientific Reports · doi:10.1038/srep17860 · Cited by 27 · see citing works
Self-citationYuki, K., Yoshida, Y., Inagaki, R., et al. (2014) · Scientific Reports · doi:10.1038/srep04568 · Cited by 24 · see citing works
Self-citationConsiderations on inhibition approaches for proinflammatory functions of ADAM proteases
Yildiz, D., & Ludwig, A. (2016) · Platelets · doi:10.1080/09537104.2016.1203396 · Cited by 24 · see citing works
Self-citationThe transformation suppressor gene Reck is required for postaxial patterning in mouse forelimbs
Yamamoto, M., Matsuzaki, T., Takahashi, R., Adachi, E., Maeda, Y., Yamaguchi, S., Kitayama, H., Echizenya, M., Morioka, Y., Alexander, D. B., et al. (2012) · Biology Open · doi:10.1242/bio.2012638 · Cited by 23 · see citing works
“5) with reduced tissue integrity and defects in vascular and neural development (Oh et al., 2001; Muraguchi et al., 2007; Chandana et al., 2010), suggesting its importance in relatively early events in mammalian development.”
BackgroundSelf-citationWang, H., Imamura, Y., Ishibashi, R., Chandana, E. P. S., Yamamoto, M., & Noda, M. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06933.x · Cited by 22 · see citing works
“3a, panel 3, bar 1) and most likely represented NPCs, whereas the Ki67-positive cells included both NPCs and other types of cells (Fig.”
BackgroundMethodInfluentialSelf-citationThe potential of RECK inducers as antitumor agents for glioma.
Chen, Y., & Tseng, S. (2012) · PubMed · Cited by 22 · see citing works
Enhancing α-secretase Processing for Alzheimer’s Disease—A View on SFRP1
Tang, B. L. (2020) · Brain Sciences · doi:10.3390/brainsci10020122 · Cited by 20 · see citing works
“Abbreviations Aβ amyloid beta; ADAM10 a disintegrin and metalloproteinase 17; AMPA receptor α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor; APP amyloid precursor protein; CSF cerebrospinal fluid; DHA docosahexaenoic acid; EGCG catechin (−)-epigallocatechin-3-gallate; HAP1 huntingtin-associated protein 1…”
BackgroundIGF-IR in neuroprotection and brain tumors
Gualco, E. (2009) · Frontiers in bioscience · doi:10.2741/3249 · Cited by 20 · see citing works
“These neuronal ADAMs, are also responsible for cleavage –mediated activation of Notch and its ligand Delta (117-120); cleavage of collagen IV, and amyloid precursor protein (APP) - decreasing formation of the toxic β-amyloid (117); and, what is closely related with the topic of this review, tissue release of IGF-I by…”
Role of proteases in dysfunctional placental vascular remodelling in preeclampsia
Gutiérrez, J., Gómez, I., Chiarello, D. I., et al. (2019) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2019.04.004 · Cited by 19 · see citing works
Isolation and characterization of novelRECKtumor suppressor gene splice variants
Trombetta-Lima, M., Winnischofer, S. M. B., Demasi, M. A. A., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.5305 · Cited by 19 · see citing works
Density- and serum-dependent regulation of the Reck tumor suppressor in mouse embryo fibroblasts
Hatta, M., Matsuzaki, T., Morioka, Y., et al. (2009) · Cellular Signalling · doi:10.1016/j.cellsig.2009.08.005 · Cited by 19 · see citing works
Self-citationMendes, S. R., del Amo-Maestro, L., Marino‐Puertas, L., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-63338-4 · Cited by 18 · see citing works
Adam10 haploinsufficiency causes freckle‐like macules in Hairless mice
Tharmarajah, G., Faas, L., Reiß, K., Säftig, P., Young, A. R., & Raamsdonk, C. D. V. (2012) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2012.01032.x · Cited by 17 · see citing works
“Interestingly, Adam10 also act as a sheddase for Delta proteins, which serve as Notch ligands (Muraguchi et al., 2007).”
BackgroundRECK Is Up-Regulated and Involved in Chondrocyte Cloning in Human Osteoarthritic Cartilage
Kimura, T., Okada, A., Yatabe, T., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.091003 · Cited by 17 · see citing works
Self-citationRECK in Neural Precursor Cells Plays a Critical Role in Mouse Forebrain Angiogenesis
Li, H., Miki, T., de Almeida, G. M., Hanashima, C., Matsuzaki, T., Kuo, C. J., Watanabe, N., & Noda, M. (2019) · iScience · doi:10.1016/j.isci.2019.08.009 · Cited by 16 · see citing works
Self-citationWhat We Learn From Transformation Suppressor Genes: Lessons From RECK
Noda, M., Takahashi, C., Matsuzaki, T., & Kitayama, H. (2010) · Future Oncology · doi:10.2217/fon.10.80 · Cited by 15 · see citing works
“Nevertheless, partially purified, soluble RECK protein (the COOH-terminal GPI-signal was eliminated) expressed in mammalian cells in suspension culture has been useful in demonstrating its ability to inhibit MMP-2, MMP-9, MT1MMP/MMP-14, CD13 and ADAM10 [24,25,29,30].”
BackgroundSelf-citationRECK-Mediated β1-Integrin Regulation by TGF-β1 Is Critical for Wound Contraction in Mice
Gutiérrez, J., Droppelmann, C. A., Contreras, O., Takahashi, C., & Brandan, E. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135005 · Cited by 15 · see citing works
Self-citationRat forming incisor requires a rigorous ECM remodeling modulated by MMP/RECK balance
Paiva, K. B. S., Zambuzzi, W. F., Accorsi-Mendonça, T., et al. (2009) · Journal of Molecular Histology · doi:10.1007/s10735-009-9231-4 · Cited by 15 · see citing works
“entiated (Echizenya et al. 2005; Kawashima et al. 2008; Kondo et al. 2007; Muraguchi et al. 2007).”
BackgroundInfluentialSharma, D., & Singh, N. K. (2021) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2021_67 · Cited by 14 · see citing works
Regional expression of the ADAMs in developing chicken cochlea
Yan, X., Lin, J., Wang, H., Markus-Koch, A., Wree, A., Rolfs, A., & Luo, J. (2010) · Developmental Dynamics · doi:10.1002/dvdy.22360 · Cited by 14 · see citing works
“ADAM10 sheds Notch ligands and regulates Notch signaling, which plays a critical role in embryonic development (Muraguchi et al., 2007).”
BackgroundSoluble Delta-like ligand 1 alters human endometrial epithelial cell adhesive capacity
Sinderen, M. L. V., Oyanedel, J., Menkhorst, E. M., et al. (2015) · Reproduction Fertility and Development · doi:10.1071/rd15313 · Cited by 14 · see citing works
“Although little is known about its function, there is some evidence that sDLL1 inhibits Notch signalling (MishraGorur et al. 2002; Muraguchi et al. 2007).”
BackgroundZhang, X., Healy, C., & Nothnick, W. B. (2012) · Endocrine · doi:10.1007/s12020-012-9614-2 · Cited by 13 · see citing works
Structure of the RECK CC domain, an evolutionary anomaly
Chang, T.-H., Hsieh, F.-L., Smallwood, P. M., Gabelli, S. B., & Nathans, J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2006332117 · Cited by 13 · see citing works
“RECK possesses matrix metalloproteinase inhibitor activity (6), and one mechanism of RECK action is via its inhibition of metalloproteinase-dependent release of NOTCH ligands from the plasma membrane (2).”
BackgroundKilic, T., Okuno, K., Eguchi, S., & Kassiri, Z. (2022) · Hypertension · doi:10.1161/hypertensionaha.122.17963 · Cited by 13 · see citing works
Dashek, R. J., Cunningham, R. P., Taylor, C. L., et al. (2024) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2024.101365 · Cited by 12 · see citing works
“Previous literature has linked RECK with suppression of ADAM10 and ADAM17 activity, 6,7 and AREG release from its cellular-membrane-anchored location.”
BackgroundNotch directly regulates cell morphogenesis genes, Reck, talin and trio, in adult muscle progenitors
Pézeron, G., Millen, K., Boukhatmi, H., & Bray, S. J. (2014) · Journal of Cell Science · doi:10.1242/jcs.151787 · Cited by 11 · see citing works
“cortical progenitors,) expression of RECK has been found to activate Notch signalling by directly inhibiting ADAM10dependent processing of Notch ligands (Muraguchi et al., 2007).”
Background
- Authors
- Muraguchi, T., Takegami, Y., Ohtsuka, T., Kitajima, S., Chandana, E. P. S., Omura, A., Miki, T., Takahashi, R., Matsumoto, N., Ludwig, A., Noda, M., & Takahashi, C.
- Affiliations
- Kyoto University (JP)
- Universitätsklinikum Aachen (DE)
- Corresponding author
- Takahashi, Chiaki
- ORCID
- Venue
- Nature Neuroscience
- Published
- 2007-06-10
- Volume
- 10
- Issue
- 7
- Pages
- 838-845
- ISSN
- 1097-6256 (ISSN-L)
- 1546-1726
- OpenAlex
- W2106253300
- Semantic Scholar
- f3ef88ae41469dd446e1434a82fe93b56e40c1ad
- Cited by
- 149
- References
- 50
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 6 · 2023: 4 · 2022: 5 · 2021: 8 · 2020: 7 · 2019: 8 · 2018: 8 · 2017: 5 · 2016: 5 · 2015: 11 · 2014: 7 · 2013: 9 · 2012: 11
- FWCI
- 3.73
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Neuroscience (publishedVersion)
- PubMed (publishedVersion)
- Kyoto University Research Information Repository (Kyoto University) (submittedVersion)
- RWTH Publications (RWTH Aachen) (submittedVersion)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Keywords
- RECK, Notch signaling, ADAM10, ectodomain shedding, Notch ligands, cortical neurogenesis, neural progenitor cells, nestin, self-renewal, brain development, protease inhibition
- MeSH terms
- ADAM10 Protein, Animals, Central Nervous System, Cerebral Cortex, Female, Fluorescent Antibody Technique, Ligands, Luciferases, Membrane Glycoproteins, Membrane Proteins, Mice, Inbred C57BL, Neurons, Phenotype, Plasmids, Pregnancy, Recombinant Proteins, Retroviridae, Immunoblotting, Signal Transduction, Down-Regulation, Mice, Knockout, Reverse Transcriptase Polymerase Chain Reaction, RNA Interference, Immunoprecipitation, Mice, ADAM Proteins, Receptors, Notch, Amyloid Precursor Protein Secretases, GPI-Linked Proteins
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