Faculty Profiles - MATURANA Andres Daniel

Papers - MATURANA Andres Daniel

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In Silico Binding Mode Analysis of Blarina Paralytic Peptides with the Human T-Type Ca Channel hCav3.2 Invited Reviewed Open Access

Nozomi Hara, Chihiro Sadamoto, Ryo Fukuoka, Yusuke Yano, Andres D Maturana, Masaki Kita

Toxins (Basel) Vol. 17 ( 11 ) page： 549 2025.11

Hyperpolarization Modulation of the T-Type hCav3.2 Channel by Human Synenkephalin [1-53], a Shrew Neurotoxin Analogue without Paralytic Effects Invited Reviewed Open Access

Ryo Fukuoka, Yusuke Yano, Nozomi Hara, Chihiro Sadamoto, Andres D. Maturana, Masaki Kit

Angewandte Chemie International Edition Vol. 64 page： e202503891 2025.7

Effects of aging on calcium channels in skeletal muscle Reviewed Open Access

Mingyi Dong and Maturana Andres

Frontiers in Molecular Biosciences Vol. 12 page： 1558456 2025.3

Glu592 of the axon guidance receptor ROBO3 mediates a pH-dependent interaction with NELL2 ligand Reviewed Open Access

Kimihiko Mizutani , Mayuko Toyoda , Teruyo Ojima-Kato, Andrés D Maturana, Tomoaki Niimi

FEBS Letters Vol. 599 ( 4 ) page： 571 - 580 2025.2

Mammalian neurotoxins, Blarina paralytic peptides, cause hyperpolarization of human T-type Ca channel hCa(v)3.2 activation. Reviewed Open Access

Yano Y, Fukuoka R, Maturana AD, Ohdachi SD, Kita M

The Journal of biological chemistry Vol. 299 ( 9 ) page： 105066 2023.7

Language：English Publishing type：Research paper (scientific journal) Publisher：Journal of Biological Chemistry

Among the rare venomous mammals, the short-tailed shrew Blarina brevicauda has been suggested to produce potent neurotoxins in its saliva to effectively capture prey. Several kallikrein-like lethal proteases have been identified, but the active substances of B. brevicauda remained unclear. Here, we report Blarina paralytic peptides (BPPs) 1 and 2 isolated from its submaxillary glands. Synthetic BPP2 showed mealworm paralysis and a hyperpolarization shift (−11 mV) of a human T-type Ca2+ channel (hCav3.2) activation. The amino acid sequences of BPPs were similar to those of synenkephalins, which are precursors of brain opioid peptide hormones that are highly conserved among mammals. However, BPPs rather resembled centipede neurotoxic peptides SLPTXs in terms of disulfide bond connectivity and stereostructure. Our results suggested that the neurotoxin BPPs were the result of convergent evolution as homologs of nontoxic endogenous peptides that are widely conserved in mammals. This finding is of great interest from the viewpoint of the chemical evolution of vertebrate venoms.

DOI： 10.1016/j.jbc.2023.105066

Open Access

Scopus

PubMed

ALPL-1 is a target for chimeric antigen receptor therapy in osteosarcoma Reviewed International coauthorship Open Access

Mensali Nadia, Koeksal Hakan, Joaquina Sandy, Wernhoff Patrik, Casey Nicholas P., Romecin Paola, Panisello Carla, Rodriguez Rene, Vimeux Lene, Juzeniene Asta, Myhre Marit R., Fane Anne, Ramirez Carolina Castilla, Maggadottir Solrun Melkorka, Duru Adil Doganay, Georgoudaki Anna-Maria, Grad Iwona, Maturana Andres Daniel, Gaudernack Gustav, Kvalheim Gunnar, Carcaboso Angel M., de Alava Enrique, Donnadieu Emmanuel, Bruland Oyvind S., Menendez Pablo, Inderberg Else Marit, Waelchli Sebastien

NATURE COMMUNICATIONS Vol. 14 ( 1 ) page： 3375 2023.6

Language：English Publishing type：Research paper (scientific journal) Publisher：Nature Communications

Osteosarcoma (OS) remains a dismal malignancy in children and young adults, with poor outcome for metastatic and recurrent disease. Immunotherapies in OS are not as promising as in some other cancer types due to intra-tumor heterogeneity and considerable off-target expression of the potentially targetable proteins. Here we show that chimeric antigen receptor (CAR) T cells could successfully target an isoform of alkaline phosphatase, ALPL-1, which is highly and specifically expressed in primary and metastatic OS. The target recognition element of the second-generation CAR construct is based on two antibodies, previously shown to react against OS. T cells transduced with these CAR constructs mediate efficient and effective cytotoxicity against ALPL-positive cells in in vitro settings and in state-of-the-art in vivo orthotopic models of primary and metastatic OS, without unexpected toxicities against hematopoietic stem cells or healthy tissues. In summary, CAR-T cells targeting ALPL-1 show efficiency and specificity in treating OS in preclinical models, paving the path for clinical translation.

DOI： 10.1038/s41467-023-39097-x

Conformational Change of the Hairpin-like-structured Robo2 Ectodomain Allows NELL1/2 Binding Reviewed Open Access

Miyaguchi Masaki, Nakanishi Yoichi, Maturana Andres D., Mizutani Kimihiko, Niimi Tomoaki

JOURNAL OF MOLECULAR BIOLOGY Vol. 434 ( 19 ) page： 167777 2022.10

Language：English Publishing type：Research paper (scientific journal) Publisher：Journal of Molecular Biology

Since neural epidermal growth factor-like-like (NELL) 2 was identified as a novel ligand for the roundabout (Robo) 3 receptor, research on NELL–Robo signaling has become increasingly important. We have previously reported that Robo2 can bind to NELL1/2 in acidic conditions but not at neutral pH. The NELL1/2-binding site that is occluded in neutral conditions is thought to be exposed by a conformational change of the Robo2 ectodomain upon exposure to acidic pH; however, the underlying structural mechanisms are not well understood. Here, we investigated the interaction between the immunoglobulin-like domains and fibronectin type III domains that form hairpin-like structure of the Robo2 ectodomain, and demonstrated that acidic pH attenuates the interaction between them. Alternative splicing isoforms of Robo2, which affect the conformation of the hairpin-like structure, were found to have distinct NELL1/2-binding affinities. We developed Förster resonance energy transfer-based indicators for monitoring conformational change of the Robo2 ectodomain by individually inserting donor and acceptor fluorescent proteins at its ends. These experiments revealed that the ends of the Robo2 ectodomain are close to each other in acidic conditions. By combining these findings with the results of size exclusion chromatography analysis, we suggest that, in acidic conditions, the Robo2 ectodomain has a compact conformation with a loose hairpin-like structure. These results may help elucidate the signaling mechanisms resulting from the interaction between Robo2 and NELL1/2 in acidic conditions.

DOI： 10.1016/j.jmb.2022.167777

Cryo-EM structures of thylakoid-located voltage-dependent chloride channel VCCN1 Reviewed International coauthorship Open Access

Tatsuya Hagino, Takafumi Kato, Go Kasuya, Kan Kobayashi, Tsukasa Kusakizako, Shin Hamamoto, Tomoaki Sobajima, Yuichiro Fujiwara, Keitaro Yamashita, Hisashi Kawasaki, Andrés D. Maturana, Tomohiro Nishizawa, Osamu Nureki

Nature Communications Vol. 13 ( 1 ) page： 2505 2022.5

Language：English Publishing type：Research paper (scientific journal) Publisher：Springer Science and Business Media LLC

Abstract

In the light reaction of plant photosynthesis, modulation of electron transport chain reactions is important to maintain the efficiency of photosynthesis under a broad range of light intensities. VCCN1 was recently identified as a voltage-gated chloride channel residing in the thylakoid membrane, where it plays a key role in photoreaction tuning to avoid the generation of reactive oxygen species (ROS). Here, we present the cryo-EM structures of Malus domestica VCCN1 (MdVCCN1) in nanodiscs and detergent at 2.7 Å and 3.0 Å resolutions, respectively, and the structure-based electrophysiological analyses. VCCN1 structurally resembles its animal homolog, bestrophin, a Ca<sup>2+</sup>-gated anion channel. However, unlike bestrophin channels, VCCN1 lacks the Ca<sup>2+</sup>-binding motif but instead contains an N-terminal charged helix that is anchored to the lipid membrane through an additional amphipathic helix. Electrophysiological experiments demonstrate that these structural elements are essential for the channel activity, thus revealing the distinct activation mechanism of VCCN1.

DOI： 10.1038/s41467-022-30292-w

Other Link： https://www.nature.com/articles/s41467-022-30292-w

The structure of MgtE in the absence of magnesium provides new insights into channel gating. Reviewed International coauthorship Open Access

Jin F, Sun M, Fujii T, Yamada Y, Wang J, Maturana AD, Wada M, Su S, Ma J, Takeda H, Kusakizako T, Tomita A, Nakada-Nakura Y, Liu K, Uemura T, Nomura Y, Nomura N, Ito K, Nureki O, Namba K, Iwata S, Yu Y, Hattori M

PLoS biology Vol. 19 ( 4 ) page： e3001231 2021.4

Id2 Represses Aldosterone-Stimulated Cardiac T-Type Calcium Channels Expression Reviewed International coauthorship Open Access

Ito J, Minemura T, Wälchli S, Niimi T, Fujihara Y, Kuroda S, Takimoto K, Maturana AD.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol. 22 ( 7 ) page： 3561 2021.3

Time-resolved serial femptosecond crystallography reveals early structural changes in channelrhodopsin. Reviewed International coauthorship Open Access

67 Oda K, Nomura T, Nakane T, Yamashita K, Inoue K, Ito S, Vierock J, Hirata K, Maturana AD, Katayama K, Ikuta T, Ishigami I, Izume T, Umeda R, Eguma R, Oishi S, Kasuya G, Kato T, Kusakizako T, Shihoya W, Shimada H, Takatsuji T, Takemoto M, Taniguchi R, Tomita A, Nakamura R, Fukuda M, Miyauchi H, Lee Y, Nango E, Tanaka R, Tanaka T, Sugahara M, Kimura T, Shimamura T, Fujiwara T, Yamanaka Y, Owada S, Joti Y, Tono K, Ishitani R, Hayashi S, Kandori H, Hegemann P, Iwata S, Kubo M, Nishizawa T, Nureki O.

eLife Vol. 10 ( e62389 ) page： 1 - 21 2021.3

アルコール飲料製造における生物学的プロセス

アンドレスマツラナ

アジア遊学 Vol. 250 page： 192 - 205 2020.8

RBM20 Regulates CaV1.2 Surface Expression by Promoting Exon 9*Inclusion of CACNA1C in Neonatal Rat Cardiomyocytes Reviewed Open Access

Morinaga Akihito, Ito Jumpei, Niimi Tomoaki, Maturana Andres D.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol. 20 ( 22 ) 2019.11

Therapeutic potential for miR-133a/b to prevent Zinc Finger Homeobox 3 loss of function-dependent Atrial Fibrillation Invited Reviewed Open Access

Maturana AD

Acta Physiologica Vol. 227 page： e13322 2019.8

Robo2 contains a cryptic binding site for neural EGFL-like (NELL) protein 1/2 Reviewed Open Access

Yamamoto Naoka, Kashiwagi Manabu, Ishihara Manami, Kojima Takaaki, Maturana Andres D., Kuroda Shun'ichi, Niimi Tomoaki

JOURNAL OF BIOLOGICAL CHEMISTRY Vol. 294 ( 12 ) page： 4693-4703 2019.3

Structural Basis of H+-Dependent Conformational Change in a Bacterial MATE Transporter Open Access

Kusakizako Tsukasa, Claxton Derek P., Tanaka Yoshiki, Maturana Andre S. D., Kuroda Teruo, Ishitani Ryuichiro, Mchaourab Hassane S., Nureki Osamu

STRUCTURE Vol. 27 ( 2 ) page： 293 - + 2019.2

MicroRNA-204 Is Necessary for Aldosterone-Stimulated T-Type Calcium Channel Expression in Cardiomyocytes Reviewed International coauthorship Open Access

Koyama Riko, Mannic Tiphaine, Ito Jumpei, Amar Laurence, Zennaro Maria-Christina, Rossier Michel Florian, Maturana Andres Daniel

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol. 19 ( 10 ) 2018.10

Functional roles of Mg binding sites in ion-dependent gating of a Mg2+ channel Mg2+, revealed by solution NMR Open Access

Maruyama Tatsuro, Imai Shunsuke, Kusakizako Tsukasa, Hattori Motoyuki, Ishitani Ryuichiro, Nureki Osamu, Ito Koichi, Maturana Andres D., Shimada Ichio, Osawa Masanori

ELIFE Vol. 7 2018.4

Electrophysiological analysis of ion channels Invited

Maturana Andres Daniel

Journal of Clinical and Experimental Medicine Vol. 262 ( 5 ) page： 506-514 2017.7

Evidence of involvement of neurone-glia/neurone-neurone communications via gap junctions in synchronised activity of KNDy neurones Reviewed

Ikegami K., Minabe S., Ieda N., Goto T., Sugimoto A., Nakamura S., Inoue N., Oishi S., Maturana A. D., Sanbo M., Hirabayashi M., Maeda K-I, Tsukamura H., Uenoyama Y.

JOURNAL OF NEUROENDOCRINOLOGY Vol. 29 ( 6 ) 2017.6

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Papers - MATURANA Andres Daniel