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Efficient targeting of membrane proteins from the endoplasmic reticulum (ER) to the inner nuclear membrane depends on GTP hydrolysis by Atlastin GTPases and their function in maintaining an interconnected topology of the ER network.

Biochemical dissections show that the Guided Entry of Tail Anchored proteins (GET) pathway selects ER-destined tail-anchored proteins using at least two distinct molecular mechanisms, each recognizing a distinct physicochemical feature in the substrate.

Sites at which mitochondria contact the endoplasmic reticulum co-localize the replication of mitochondria and their DNA to help ensure that DNA is distributed appropriately between the newly formed organelles in cells.

A cell-free biochemical assay for protein lipidation identifies the ER–Golgi intermediate compartment as a key early station in the formation of an autophagosome.

Imaging, quantitative immunoblotting and mass spectrometry reveal that hundreds of surface-expressed neuronal membrane proteins exhibit atypical glycosylation profiles, resulting in changes in protein half-life and synaptic responses.

STIM1 regulates the contractility of blood vessels and blood pressure by organizing membrane contact sites and ion channel activity in vascular smooth muscle cells in a manner that is independent of its canonical function in store-operated Ca²⁺entry.

The lipid kinase VPS34 complexes I and II are both activated by unsaturation of substrate and non-substrate lipids, curvature, electrostatics and polyphosphoinositides, which play roles in localisation and cellular function.

One minute biotinylation with APEX2 peroxidase in living cells identifies established and new components of mitochondrial and ER membranes; dataset intersection and overexpression screen identifies SYNJ2BP overexpression as inducing mitochondria-rough ER contacts.

Src phosphorylates GBF1, promoting binding of the Sec7 domain to Arf1 and the formation of GALNTs containing tubules emanating from the Golgi.

ABHD16A is a phospholipid-modifying endoplasmic reticulum (ER) membrane protein required for both mitochondrial fission and fusion machinery recruitment to ER-associated mitochondrial constrictions.