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Identification of p115 interacting proteins from HEK293T cells

ABSTRACT: The protein p115 is a key player in the delivery of vesicles from the endoplasmic reticulum to the early Golgi. The protein is a homodimer with a folded head domain and a coiled-coil tail that is anchored to Golgi membranes. p115 has been shown to capture vesicles and to bind to SNARE proteins to promote membrane fusion. This project was to look for more interaction partners of p115 by expressing GFP fusions to the full length protein or to either the head or the tail alone. These fusions were expressed in HEK293T cells and co-precipitating proteins identified by mass-spectrometry and compared to those found with precipitation of GFP alone.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Catarina de Matos Ferraz Franco

LAB HEAD: Sean Munro

PROVIDER: PXD075617 | Pride | 2026-06-02

REPOSITORIES: Pride

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			Action	DRS
	OMG5379.sf3	Other
	OMG5379A10LC2_B2.raw	Raw
	OMG5379A11LC2_C2.raw	Raw
	OMG5379A12LC2_D2.raw	Raw
	OMG5379A13LC2_E2.raw	Raw

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Publications

The Golgi vesicle tether p115/USO1 can bind directly to the ER exit site organiser Sec16A.

Yakunin Igor I Gillingham Alison K AK Pereira Conceição C Gershlick David C DC Munro Sean S

Journal of cell science 20260522

Newly made secretory and membrane proteins exit the endoplasmic reticulum (ER) in COPII vesicles that form at specialised ER exit sites. These exit sites are typically near to the early Golgi compartments that receive these vesicles. A key player in the delivery of vesicles to the early Golgi is p115 (USO1), a homodimer with a folded head domain and a coiled-coil tail that is anchored to Golgi membranes. p115 has been shown to capture vesicles and to bind to SNARE proteins to promote membrane fu ...[more]

PMID: 42169630

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