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SIDT2 Associates with Apolipoprotein A1 (ApoA1) and Facilitates ApoA1 Secretion in Hepatocytes.

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Sampieri, Alicia 
Asanov, Alexander 
Méndez-Acevedo, Kevin Manuel  ORCID logo


SIDT2 is a lysosomal protein involved in the degradation of nucleic acids and the transport of cholesterol between membranes. Previous studies identified two "cholesterol recognition/interaction amino acid consensus" (CRAC) motifs in SIDT1 and SIDT2 members. We have previously shown that the first CRAC motif (CRAC-1) is essential for protein translocation to the PM upon cholesterol depletion in the cell. In the present study, we show that SIDT2 and the apolipoprotein A1 (ApoA1) form a complex which requires the second CRAC-2 motif in SIDT2 to be established. The overexpression of SIDT2 and ApoA1 results in enhanced ApoA1 secretion by HepG2 cells. This is not observed when overexpressing the SIDT2 with the CRAC-2 domain mutated to render it unfunctional. All these results provide evidence of a novel role for SIDT2 as a protein forming a complex with ApoA1 and enhancing its secretion to the extracellular space.


Peer reviewed: True

Acknowledgements: We would like to thank the imaging and molecular biology units from the Instituto de Fisiologia Celular for their technical support on the use of equipment and for DNA sequencing. We acknowledge the invaluable support from the unidad de computo from the Instituto de Fisiologia Celular.

Funder: Instituto de Fisiologia Celular


ApoA1, CRAC motif, SIDT2, cholesterol, Apolipoprotein A-I, Protein Transport, Hepatocytes, Cholesterol, Lysosomes

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Direccion General de Asuntos del Personal Academico (IN206323)