Surfaceome dynamics reveal proteostasis-independent reorganization of neuronal surface proteins during development and synaptic plasticity.
IF: 17.694
Cited by: 21


Neurons are highly compartmentalized cells with tightly controlled subcellular protein organization. While brain transcriptome, connectome and global proteome maps are being generated, system-wide analysis of temporal protein dynamics at the subcellular level are currently lacking. Here, we perform a temporally-resolved surfaceome analysis of primary neuron cultures and reveal dynamic surface protein clusters that reflect the functional requirements during distinct stages of neuronal development. Direct comparison of surface and total protein pools during development and homeostatic synaptic scaling demonstrates system-wide proteostasis-independent remodeling of the neuronal surface, illustrating widespread regulation on the level of surface trafficking. Finally, quantitative analysis of the neuronal surface during chemical long-term potentiation (cLTP) reveals fast externalization of diverse classes of surface proteins beyond the AMPA receptor, providing avenues to investigate the requirement of exocytosis for LTP. Our resource ( highlights the importance of subcellular resolution for systems-level understanding of cellular processes.

MeSH terms

Cell Membrane
Cells, Cultured
Excitatory Postsynaptic Potentials
Long-Term Potentiation
Membrane Proteins
Neuronal Plasticity
Protein Interaction Maps
Protein Transport


van Oostrum, Marc
Campbell, Benjamin
Seng, Charlotte
Müller, Maik
Tom Dieck, Susanne
Hammer, Jacqueline
Pedrioli, Patrick G A
Földy, Csaba
Tyagarajan, Shiva K
Wollscheid, Bernd

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