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Hanako Tsushima

Post Doc

Research Line

Genetics and Epigenetics of Behavior


IIT Central Research Labs Genova


Dept. Neuroscience and Brain Technologies Istituto Italiano di Tecnologia
+39 010 71781 509
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Date and place of birth : 11th May 1979, Tokyo, Japan

Nationality: Japanese

2010-present: Post-doctoral fellow in the research group of Dr. Evelina Chieregatti, Dept. Neuroscience and Brain Technologies, Istituto Italiano di Tecnologia, Genoa, Italy.



2002-2008: Ph.D from the Open University, UK, carried out in the laboratory of Prof. Peir Paolo Di Fiore, The European Institute of Oncology (IFOM-IEO), Milan, ItalyTitle of the PhD thesis: "A Study of the interactors of Eps15 Homology (EH) domain and the role of the EH network in the model system of Caenorhabditis elegans."

1998-2002: B.Sc 2:1 Hon.,Department of Biochemistry and Molecular Biology, University College London, University of London, UK.

1996-1998: International Baccalaureate Bilingual Diploma from the United Wolrd College of South East Asia, Singapore.



2009: Post-doctoral fellow in the research group of Dr. Evelina Chieregatti, DIBIT, Fondazione di San Raffaele, Milan,  hosted in the laboratory of Dr. Carlo Sala, Institute of Neuroscience, CNR, Milan, Italy

2002: BSc thesis in the laboratories of Dr. Anne Ridley and of Dr. Rainer Cramer, Ludwig Institute of Cancer Research, London, UK. Project on identification of the phosphorylation of RhoE by ROCK using peptide mass finger printing with MALDI-ToF.

2000-2001: Industrial placement under the supervision of Dr. Klaus Schneider at the Department of Computational and Structural Sciences, GlaxoSmithKline Pharmaceuticals, Harlow, UK.



Pathogenesis of Brain diseases, Molecular Neurobiology, Dept. of Neuroscience and Brain Technologies

Introduction: The presence of  amyloid plaques, together with neurofibrillary tangles are considered to be the hallmarks of Alzheimer’s Disease (AD). A major consitutent of amyloid plaques is beta-amyloid peptide (Aß ), which derives from the proteolytic cleavage of a transmembrane protein, Amyloid Precursor Protein (APP). APP is first cleaved by the beta-secretase, BACE1 and the subsequent cleavage by the gamma secretase results in the generation of Aß .

1. Studying the effect of Aß peptide on cytoskeletal structures in neurites and growth cones of developing neurons.

A number of recent evidence points to synaptic loss and alterations in neurites morphology during the early development of AD. We are currently investigating the effect of Aß on the growth and retraction of neurites in cultured neurons.

This project focuses on the effect of monomeric Aß peptide on microtubules and actin cytoskeleton in cultured hippomcampal neurons. We follow the modification on actin dynamics and microtubule stability upon incubation with Aß by various imaging techniques as well as biochemical approach. We are currently studying the involvement of membrane microdomains, such as lipid raft, in the molecular mechanism underlying these cytoskeletal changes.

Together with Alpha-synuclein (α-syn), Aβ is also a major component of fibrillary lesions such as Lewy bodies and amyloid plaques of other neurodegenerative disorders, such as Parkinson’s disease (PD). A possible interplay between these two amyloidogenic components has been suggested by several studies. Using cultured neurons from wild type and from a deletion mutant of α-syn, we are also investigating the role of α-syn in the effects induced by Aß.

2. Identification of proteins that are internalized with Amyloid Precursor Protein (APP) by immunoisolation of APP-containing endocytic vesicles.

The intracellular localization of the cleavage of APP by BACE1 has long been a topic of debate. Although both proteins, APP and BACE1 are found as transmembrane proteins, numerous evidence suggest that amyloidogenesis increases with enhanced endocytosis. Early endosome is the first site of APP endocytic sorting, where APP has been shown to co-localize with BACE1 by more recent studies. Altered endosomal structures in AD brains have also become another characteristic of AD.

With these observations pointing towards the importance of APP-containing endosomes in the pathology of AD, we are using proteomic approaches to identify proteins of interest such as molecular motors,enzymes or adaptor proteins that may be found in the APP-containing endocytic vesicles.

Selected Publications

Tsushima H, Emanuele, M, Esposito A, Polenghi A, Vassalli M, Barberis A, Difato F & Chieregatti E. 
HDAC6 and RhoA are novel players in Abeta-driven disruption of neuronal polarity. Nat. Commun. 6:7781 doi:10.1038/ncomms8781, 2015

Bellani S, Mescola A, Ronzitti G, Tsushima H, Tilve S, Canale C, Valtorta F, Chieregatti E.
GRP78 clustering at the cell surface of neurons transduces the action of exogenous alpha-synuclein.
Cell Death Differ. doi:10/1038/cdd.2014.111, 2014

Tsushima H, Malabarba MG, Confalonieri S, Senic-Matuglia F, Verhoef LGGC, Bartocci C, D'Ario G, Cocito A, Di Fiore PP and Salcini AE  (2013)
A Snapshot of the Physical and Functional Wiring of the Eps15 Homology Domain Network in the Nematode. PLoS ONE 8(2): e56383. doi:10.1371/journal.pone.0056383.

Beke S, Anjum F, Tsushima H, Ceseracciu L, Chieregatti E, Diaspro A, Athanassiou A, and Brandi F.
Towards excimer-laser-based stereolithography: a rapid process to fabricate rigid biodegradable photopolymer scaffolds
J. R. Soc. Interface doi:10.1098/rsif.2012.0300, 2012

Difato F, Tsushima H, Pesce M, Benfenati F, Blau A, and Chieregatti E.
The Formation of actin waves during regeneration after axonal lesion is enhanced by BDNF. Sci.Rep. 1, 183; DOI:10.1038/srep00183, 2011

Rose S, Malabarba MG, Krag C, Scultz A, Tsushima H, Di Fiore, P and Salcini AE.
Caenorhabditis elegans intersectin: a synaptic protein regulating neurotransmission. Mol.Biol.Cell, 18(12):5091-9, 2007




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I numeri di IIT

L’Istituto Italiano di Tecnologia (IIT) è una fondazione di diritto privato - cfr. determinazione Corte dei Conti 23/2015 “IIT è una fondazione da inquadrare fra gli organismi di diritto pubblico con la scelta di un modello di organizzazione di diritto privato per rispondere all’esigenza di assicurare procedure più snelle nella selezione non solo nell’ambito nazionale dei collaboratori, scienziati e ricercatori ”.

IIT è sotto la vigilanza del Ministero dell'Istruzione, dell'Università e della Ricerca e del Ministero dell'Economia e delle Finanze ed è stato istituito con la Legge 326/2003. La Fondazione ha l'obiettivo di promuovere l'eccellenza nella ricerca di base e in quella applicata e di favorire lo sviluppo del sistema economico nazionale. La costruzione dei laboratori iniziata nel 2006 si è conclusa nel 2009.

Lo staff complessivo di IIT conta circa 1440 persone. L’area scientifica è rappresentata da circa l’85% del personale. Il 45% dei ricercatori proviene dall’estero: di questi, il 29% è costituito da stranieri provenienti da oltre 50 Paesi e il 16% da italiani rientrati. Oggi il personale scientifico è composto da circa 60 principal investigators, circa 110 ricercatori e tecnologi di staff, circa 350 post doc, circa 500 studenti di dottorato e borsisti, circa 130 tecnici. Oltre 330 posti su 1400 creati su fondi esterni. Età media 34 anni. 41% donne / 59 % uomini.

Nel 2015 IIT ha ricevuto finanziamenti pubblici per circa 96 milioni di euro (80% del budget), conseguendo fondi esterni per 22 milioni di euro (20% budget) provenienti da 18 progetti europei17 finanziamenti da istituzioni nazionali e internazionali, circa 60 progetti industriali

La produzione di IIT ad oggi vanta circa 6990 pubblicazioni, oltre 130 finanziamenti Europei e 11 ERC, più di 350 domande di brevetto attive, oltre 12 start up costituite e altrettante in fase di lancio. Dal 2009 l’attività scientifica è stata ulteriormente rafforzata con la creazione di dieci centri di ricerca nel territorio nazionale (a Torino, Milano, Trento, Parma, Roma, Pisa, Napoli, Lecce, Ferrara) e internazionale (MIT ed Harvard negli USA) che, unitamente al Laboratorio Centrale di Genova, sviluppano i programmi di ricerca del piano scientifico 2015-2017.

IIT: the numbers

Istituto Italiano di Tecnologia (IIT) is a public research institute that adopts the organizational model of a private law foundation. IIT is overseen by Ministero dell'Istruzione, dell'Università e della Ricerca and Ministero dell'Economia e delle Finanze (the Italian Ministries of Education, Economy and Finance).  The Institute was set up according to Italian law 326/2003 with the objective of promoting excellence in basic and applied research andfostering Italy’s economic development. Construction of the Laboratories started in 2006 and finished in 2009.

IIT has an overall staff of about 1,440 people. The scientific staff covers about 85% of the total. Out of 45% of researchers coming from abroad 29% are foreigners coming from more than 50 countries and 16% are returned Italians. The scientific staff currently consists of approximately 60 Principal Investigators110 researchers and technologists350 post-docs and 500 PhD students and grant holders and 130 technicians. External funding has allowed the creation of more than 330 positions . The average age is 34 and the gender balance proportion  is 41% female against 59% male.

In 2015 IIT received 96 million euros in public funding (accounting for 80% of its budget) and obtained 22 million euros in external funding (accounting for 20% of its budget). External funding comes from 18 European Projects, other 17 national and international competitive projects and approximately 60 industrial projects.

So far IIT accounts for: about 6990 publications, more than 130 European grants and 11 ERC grants, more than 350 patents or patent applications12 up start-ups and as many  which are about to be launched. The Institute’s scientific activity has been further strengthened since 2009 with the establishment of 11 research nodes throughout Italy (Torino, Milano, Trento, Parma, Roma, Pisa, Napoli, Lecce, Ferrara) and abroad (MIT and Harvard University, USA), which, along with the Genoa-based Central Lab, implement the research programs included in the 2015-2017 Strategic Plan.