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Affinity-ranking BIN1 interactions and screening natural BIN1 variants that may cause neuromuscular disorders

ABSTRACT: Deletion of the protein-protein interaction SH3 domain of the membrane remodeling BIN1 protein was found to lead to centronuclear myopathy in patients, yet only few interaction partners of BIN1 SH3 have been identified so far. Here we used the holdup assay to proteome-wide measure steady-state affinity constants of BIN1 SH3 domain for thousands of full-length cellular proteins, as well as for hundreds of putative SH3-binding sites found within the identified BIN1 binders. Besides confirming known partners, such as DNM2, we also identified and affinity-characterized numerous others. We also assessed the impact of a set of rare natural BIN1 SH3 domain variants on affinity interactomes and identified a set of potentially harmful ones that exhibited perturbed affinity profiles, whose impact were confirmed by cellular assay, tentatively connecting them to neuromuscular disorders.

INSTRUMENT(S): LTQ Orbitrap Elite, Q Exactive

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Jurkat Cell

SUBMITTER: Luc Negroni

LAB HEAD: Gergo Gogl

PROVIDER: PXD040169 | Pride | 2024-07-11

REPOSITORIES: Pride

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			Action	DRS
	220125_GG_Ech01_Rep1.msf	Msf
	220125_GG_Ech01_Rep1.raw	Raw
	220125_GG_Ech01_Rep2.msf	Msf
	220125_GG_Ech01_Rep2.raw	Raw
	220125_GG_Ech01_Rep3.msf	Msf

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