Goradia Group

Nishit Goradia, PhD

Group Leader

Laboratory of Transcriptional Assembly Biology
ORCID:0000-0002-7929-8991

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Research interests

Laboratory of Transcriptional Assembly Biology

Our Research

Transcription is controlled by dynamic networks of regulatory proteins that assemble within the nucleus. While many of the individual components of these networks have been identified, far less is understood about how their higher-order organization shapes gene regulation. The Goradia Lab investigates how regulatory protein assemblies control transcription and cell fate. We study how multivalent protein interactions drive the formation of molecular assemblies, how these structures are organized within the nucleus, and how they shape transcriptional programmes during development and disease. Our research seeks to define how these assemblies coordinate transcription across biological scales: from molecular interactions to tissue function.

Research Questions

How do regulatory protein assemblies form?

Transcriptional regulators rarely act alone. Instead, they interact through multivalent binding interfaces, intrinsically disordered regions, and short linear motifs to generate molecular assemblies whose properties extend beyond those of individual protein interactions. We investigate the mechanisms that govern the formation, organization, and regulation of these assemblies, and determine how their structural and dynamic properties influence transcription.

How does nuclear organization influence transcription?

The nucleus is a highly organized environment in which the spatial arrangement of regulatory proteins contributes to gene regulation. However, the mechanisms linking nuclear organization to transcriptional control remain largely unknown. We investigate how protein assemblies shape nuclear architecture and how their spatial organization influences transcription, cellular identity, and cell fate during development, tissue homeostasis, and disease.

How do molecular assemblies shape biological function?

Understanding transcription requires connecting molecular mechanisms with biological function. We therefore study regulatory protein assemblies across multiple levels of biological complexity: from purified molecular systems and cultured cells to advanced cellular models, including organoids. By integrating molecular and cell biology, biochemistry, genome engineering, quantitative imaging, functional genomics, and computational approaches, we investigate how molecular assemblies regulate gene expression in physiological and disease contexts.

Our Vision

We believe that higher-order protein assembly is a fundamental organizational principle of transcriptional regulation. Understanding how regulatory proteins assemble and function within the nucleus will reveal new mechanisms by which cells establish and maintain gene expression programmes. Our long-term vision is to establish Transcriptional Assembly Biology as a conceptual framework for understanding transcriptional regulation. We seek to bridge molecular mechanisms with cellular and tissue-level biology, uncovering how regulatory protein assemblies govern cellular identity during development and how their dysregulation contributes to cancer and other human diseases. By integrating mechanistic studies with advanced cellular models, we aim to define general principles by which protein assemblies coordinate transcription across biological systems, providing new insights into development, tissue homeostasis, and human disease.

Members of the group

NameSurnameDegreeE-mail

Publications

2024

Goradia N and Werner S (Joint first co-authors), Mullapudi E, Greimeier S, Merkens L, Lang A, Mertens H, Weglarz A, Sander S, Chojnowski G, Wikman H, Ohlenschläger O, Von Amsberg G, Pantel K and Wilmanns M. Master corepressor inactivation through multivalent SLiM-induced polymerization mediated by the oncogene suppressor RAI2. Nature communications 15:5241, 1-16.

2021

Lu S, Louphrasitthiphol P, Goradia N, Lambert JP, Schmidt J, Chauhan J, Rughani MG, Larue L, Wilmanns M and Goding CR. (2021). TBX2 controls a proproliferative gene expression program in melanoma. Genes & Development 35(23-24), 1657-1677.

2020

Lang A and Goradia N (Joint first co-authors), Wikman H, Werner S, Wilmanns M and Ohlenschläger O. (2020). 1H, 13C, and 15N backbone assignments of the C-terminal region of the human retinoic acid-induced protein 2. Biomolecular NMR assignments 14(2), 271-275.

2019

Wißbrock A and Goradia N (Joint first co-authors), Kumar A, George AAP, Kühl T, Bellstedt P, Ramachandran R, Hoffmann P, Galler K, Popp J, Neugebauer U, Hampel K, Zimmermann B, Adam S, Wiendl M, Krönke G, Hamza I, Heinemann SH, Frey S, Hüber AJ, Ohlenschläger O, and Imhof D. (2019). Structural insights into heme binding to IL-36α proinflammatory cytokine. Scientific Reports
9(1): 16893, 1-14..org/10.1101/sqb.2019.84.040295u003c/liu003ernu003c/ulu003e

2018

Kumar A, Wißbrock A, Goradia N, Bellstedt P, Ramachandran R, Imhof D, Ohlenschläger O.
(2018). Heme interaction of the intrinsically disordered N-terminal peptide segment of human
cystathionine-ß-synthase. Scientific Reports 8(1): 2474, 1-9.

2016

Goradia N, Wißbrock A, Wiedemann C, Bordusa F, Ramachandran R, Imhof D, Ohlenschläger,
O (2016). 1 H, 13 C, and 15 N resonance assignments for the pro-inflammatory cytokine interleukin-36α. Biomolecular NMR assignments 10(2), 329-333.

2015

Brewitz H, Goradia N, Schubert E, Galler K, Kühl T, Syllwasschy B, Popp J, Neugebauer U,
Hagelueken G, Schiemann O, Ohlenschläger O and Imhof D. (2015). Heme interacts with
histidine- and tyrosine-based protein motifs and inhibits enzymatic activity of Chloramphenicol acetyltransferase from E.coli. Biochimica et Biophysica Acta (BBA) 1860, 1343-1353.

Wiedemann C, Goradia N, Häfner S, Herbst C, Görlach M, Ohlenschläger O, Ramachandran
R. (2015). HN-HCA heteronuclear TOCSY-NH experiment for 1 H N and 15 N sequential
correlations in ( 13 C, 15 N) labelled intrinsically disordered proteins. Journal of Biomolecular NMR 63, 201-212.

Brewitz H, Kühl T, Goradia N, Galler K, Popp J, Neugebauer U, Ohlenschläger O and Imhof,
D. (2015). Role of the chemical environment beyond the coordination site: Structural insights
into Fe (III) protoporphyrin binding to cysteine-based heme-regulatory protein motifs,
ChembioChem 16, 2216-2224.

Goradia N, Wiedemann C, Herbst C, Görlach M, Heinemann S, Ohlenschläger O and
Ramachandran R. (2015). An approach to NMR assignment of intrinsically disordered proteins. ChemPhysChem 16(4), 739-746.

About Group Leader

Dr Nishit Goradia received his PhD from the Leibniz Institute on Aging – Fritz Lipmann Institute in Jena, Germany, under the supervision of Dr Oliver Ohlenschläger in the laboratory of Dr Matthias Görlach. His doctoral research focused on peptide/protein–heme
interactions using biomolecular NMR and complementary biophysical approaches.

He subsequently joined the laboratory of Prof. Matthias Wilmanns at EMBL Hamburg as a postdoctoral researcher, where he employed a broad range of structural biology and biophysical approaches to investigate the molecular mechanisms of cancer-associated
proteins. During this period, he initiated his research on the interaction between the transcriptional corepressor CtBP and the tumour suppressor RAI2.

This work revealed that multivalent short linear motifs in RAI2 drive higher-order CtBP polymerization, providing a previously unrecognized mechanism for regulating CtBP transcriptional activity. He later continued this research as a Medical Scientist Fellow at the
Institute of Tumor Biology, University Medical Center Hamburg-Eppendorf (UKE), headed by Prof. Klaus Pantel, where he was hosted in the laboratory of Dr Stefan Werner. During this fellowship, he expanded his research towards cancer cell biology and advanced microscopy,
integrating these approaches with his structural and biochemical expertise.

In 2026, he established his independent research group at IMol in Warsaw. His laboratory investigates how multivalent protein interactions and higher-order molecular assemblies egulate transcription and cell fate, and how disruption of these mechanisms contributes to
cancer.

Awards

Research Prize, Hamburg Cancer Society, 2025
Awarded for the Nature Communications study on RAI2-induced CtBP polymerization.

Funding

 

2026 – 2031
  • National Science Centre, Poland (NCN) (2026-2031)
    SONATA BIS 15
    Molecular Mechanism of CtBP corepressor activity inactivation by RAI2-induced CtBP
    polymerization
    Principal Investigator
2024 – 2025
  • German Cancer Aid (Deutsche Krebshilfe) (2024-2025)
    Mildred Scheel Nachwuchszentrum Medical Scientist Fellowship
    University Medical Center Hamburg-Eppendorf
2024 – 2026
  • Roggenbuck Stiftung (2024-2026)
    Research funding supporting the CtBP–RAI2 research programme