Dataset Information

VAMP2/3-dependent membrane proteome in oligodendrocytes

ABSTRACT: Which proteins in oligodendrocytes require VAMP2/3-mediated exocytosis for membrane trafficking? We isolated primary oligodendrocytes from transgenic mice expressing oligodendrocyte-targeted botulinum toxin and littermate controls and used surface biotinylation to determine which proteins were differentially trafficked to the cell surface.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Primary Cell, Oligodendrocyte

SUBMITTER: Mable Lam

LAB HEAD: J. Bradley Zuchero

PROVIDER: PXD036174 | Pride | 2022-10-14

REPOSITORIES: Pride

ACCESS DATA

Publications

CNS myelination requires VAMP2/3-mediated membrane expansion in oligodendrocytes.

Lam Mable M Takeo Koji K Almeida Rafael G RG Cooper Madeline H MH Wu Kathryn K Iyer Manasi M Kantarci Husniye H Zuchero J Bradley JB

Nature communications 20220923 1

Myelin is required for rapid nerve signaling and is emerging as a key driver of CNS plasticity and disease. How myelin is built and remodeled remains a fundamental question of neurobiology. Central to myelination is the ability of oligodendrocytes to add vast amounts of new cell membrane, expanding their surface areas by many thousand-fold. However, how oligodendrocytes add new membrane to build or remodel myelin is not fully understood. Here, we show that CNS myelin membrane addition requires e ...[more]

PMID: 36151203

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Project description:ARHGAP36 is an atypical Rho GTPase-activating protein (GAP) family member that drives both spinal cord development and tumorigenesis, acting in part through an N-terminal motif that suppresses protein kinase A and activates Gli transcription factors. ARHGAP36 also contains isoform-specific N-terminal sequences, a central GAP-like module, and a unique C-terminal domain, and the functions of these regions remain unknown. Here we have mapped the ARHGAP36 structure-activity landscape using a deep sequencing-based mutagenesis screen and truncation mutant analyses. Using this approach, we have discovered several residues in the GAP homology domain that are essential for Gli activation and a role for the C-terminal domain in counteracting an N-terminal autoinhibitory motif that is present in certain ARHGAP36 isoforms. In addition, each of these sites modulates ARHGAP36 recruitment to the plasma membrane or primary cilium. Through comparative proteomics, we also have identified proteins that preferentially interact with active ARHGAP36, and we demonstrate that one binding partner, prolyl oligopeptidase-like protein, is a novel ARHGAP36 antagonist. Our work reveals multiple modes of ARHGAP36 regulation and establishes an experimental framework that can be applied towards other signaling proteins. This accession contains raw data from an interactome analysis of wild-type and L317P mutant ARHGAP36 isoform 2, represented in Fig. 5 and Dataset S2 of the associated publication.nactive GAP-like domain mutant, we have also identified prolyl oligopeptidase-like protein (PREPL) as a direct antagonist that decreases ARHGAP36 protein expression. In combination, our systems-level analyses uncover an ensemble of mechanisms that regulate ARHGAP36 expression, localization, and activity state, providing a potential means for context-specific ARHGAP36 functions. This accession contains raw data from an interactome analysis of wild-type and L317P mutant ARHGAP36 isoform 2, represented in Fig. 5 and Dataset S2 of the associated publication.

Dataset Information

VAMP2/3-dependent membrane proteome in oligodendrocytes

Publications

CNS myelination requires VAMP2/3-mediated membrane expansion in oligodendrocytes.

Similar Datasets

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