Louise Pinet

EDUCATION

Bachelor of chemistry - Université Pierre et Marie Curie (Now Sorbonne Université)
Master of Molecular and Cellular Biology, Specialty Biological Systems and Physical Concepts - Université Pierre et Marie Curie (Now Sorbonne Université) and Ecole Normale Supérieure de Paris
PhD of Biochemistry and Structural Biology - Institut de Chimie des Substances Naturelles CNRS UPR 2301 / Université Paris Saclay

RESEARCH INTERESTS

Biochemistry, Biophysics, NMR, Single molecule FRET, Intrinsically Disordered Proteins, Poly(ADP-ribose), Nucleosomes, Linker histone H1

Scopus Publications

Expanding the disorder-function paradigm in the C-terminal tails of erbbs
Louise Pinet, Nadine Assrir, and Carine van Heijenoort
MDPI AG
ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 years, structurally and functionally. However, their whole C-terminal tails (CTs) following the kinase domain were only described at atomic resolution in the last 4 years. They were shown to be intrinsically disordered. The CTs are known to be tyrosine-phosphorylated when the activated homo- or hetero-dimers of ErbBs are formed. Their phosphorylation triggers interaction with phosphotyrosine binding (PTB) or Src Homology 2 (SH2) domains and activates several signaling pathways controling cellular motility, proliferation, adhesion, and apoptosis. Beyond this passive role of phosphorylated domain and site display for partners, recent structural and function studies unveiled active roles in regulation of phosphorylation and interaction: the CT regulates activity of the kinase domain; different phosphorylation states have different compaction levels, potentially modulating the succession of phosphorylation events; and prolines have an important role in structure, dynamics, and possibly regulatory interactions. Here, we review both the canonical role of the disordered CT domains of ErbBs as phosphotyrosine display domains and the recent findings that expand the known range of their regulation functions linked to specific structural and dynamic features.


Structural and dynamic characterization of the C-terminal tail of ErbB2: Disordered but not random
Louise Pinet, Ying-Hui Wang, Célia Deville, Ewen Lescop, Françoise Guerlesquin, Ali Badache, François Bontems, Nelly Morellet, Dominique Durand, Nadine Assrir,et al.
Elsevier BV



¹ H, ¹³ C and ¹⁵ N assignments of human Grb2 free of ligands
Louise Pinet, Ying-Hui Wang, Anaïs Vogel, Françoise Guerlesquin, Nadine Assrir, and Carine van Heijenoort
Springer Science and Business Media LLC
AbstractGrowth factor receptor-bound 2 (Grb2) is an important link in the receptor tyrosine kinase signaling cascades. It is involved in crucial processes, both physiological (mainly embryogenesis) and pathological (different types of cancer). Several binding partners of all three domains (SH3–SH2–SH3) of this adaptor protein are well described, such as ErbB family members for the SH2 domain and Sos for the SH3 domains. How the different domains interact with each other, both structurally and functionally, is still unclear. These interactions could be essential for regulation processes, and therefore are of great interest. Although a lot of structural data on Grb2 exist, they describe either individual domains, ligand-bound conformations, or frozen pictures of the protein captured by crystallography. Here we report the assignment of backbone and of $$^{13}\\hbox {C}_\\beta$$ 13 C β chemical shifts of full-length, apo-Grb2 in solution. In addition to the assigned conformation corresponding to three well-folded domains, a set of peaks compatible with the presence of an unfolded conformation of the N-terminal SH3 domain is observed. This assignment paves the way for future studies of inter-domain interactions and dynamics that have to be taken into account when studying the regulation of Grb2 interactions and signaling pathways.


Structural Characterization of N-WASP Domain V Using MD Simulations with NMR and SAXS Data
Maud Chan-Yao-Chong, Célia Deville, Louise Pinet, Carine van Heijenoort, Dominique Durand, and Tâp Ha-Duong
Elsevier BV



¹H, ¹³C and ¹⁵N assignments of the C-terminal intrinsically disordered cytosolic fragment of the receptor tyrosine kinase ErbB2
YingHui Wang, Louise Pinet, Nadine Assrir, Latifa Elantak, Françoise Guerlesquin, Ali Badache, Ewen Lescop, and Carine van Heijenoort
Springer Science and Business Media LLC