Stomatin-like protein-1 interacts with stomatin and is targeted to late endosomes.
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STOML1 localizes to late endosomes/multivesicular bodies, not plasma membrane
"We show here that SLP-1 localizes to the late endosomal compartment, like stomatin. Unlike stomatin, SLP-1 does not localize to the plasma membrane."
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Contains N-terminal GYXXF sorting signal essential for late endosomal targeting
"We found that the targeting of SLP-1 to late endosomes is caused by a GYXXPhi (Phi being a bulky, hydrophobic amino acid) sorting signal at the N terminus."
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Mutation of sorting signal redirects protein to plasma membrane
"Mutation of this signal results in plasma membrane localization."
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Interacts directly with stomatin via co-immunoprecipitation
"We proved the postulated interaction of SLP-1 with stomatin by co-immunoprecipitation and localized the interaction site to the conserved stomatin part of SLP-1."
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Associates with detergent-resistant membranes (lipid rafts)
"SLP-1 and stomatin co-localize in the late endosomal compartment, they co-immunoprecipitate, thus showing a direct interaction, and they associate with detergent-resistant membranes."
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SCP-2 domain involved in cholesterol transfer to late endosomes
"This massive cholesterol accumulation clearly depends on the SCP-2 domain of SLP-1, suggesting a role for this domain in cholesterol transfer to late endosomes."
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Under blocked cholesterol efflux, induces enlarged cholesterol-filled vesicles
"In accordance with the proposed lipid transfer function, we show that, under conditions of blocked cholesterol efflux from late endosomes, SLP-1 induces the formation of enlarged, cholesterol-filled, weakly LAMP-2-positive, acidic vesicles in the perinuclear region."