Abstract:
:GABARAPL1 belongs to the small family of GABARAP proteins (including GABARAP, GABARAPL1 and GABARAPL2/GATE-16), one of the two subfamilies of the yeast Atg8 orthologue. GABARAPL1 is involved in the intracellular transport of receptors, via an interaction with tubulin and GABA(A) or kappa opioid receptors, and also participates in autophagy and cell proliferation. In the present study, we identify the HSP90 protein as a novel interaction partner for GABARAPL1 using GST pull-down, mass spectrometry and coimmunoprecipitation experiments. GABARAPL1 and HSP90 partially colocalize in MCF-7 breast cancer cells overexpressed Dsred-GABARAPL1 and in rat brain. Moreover, treatment of MCF-7 cells overexpressed FLAG-GABARAPL1-6HIS with the HSP90 inhibitor 17-AAG promotes the GABARAPL1 degradation, a process that is blocked by proteasome inhibitors such as MG132, bortezomib and lactacystin. Accordingly, we demonstrate that HSP90 interacts and protects GABARAPL1 from its degradation by the proteasome.
journal_name
Biochimiejournal_title
Biochimieauthors
Seguin-Py S,Lucchi G,Croizier S,Chakrama FZ,Despouy G,Le Grand JN,Ducoroy P,Boireau W,Boyer-Guittaut M,Jouvenot M,Fraichard A,Delage-Mourroux Rdoi
10.1016/j.biochi.2011.11.006subject
Has Abstractpub_date
2012-03-01 00:00:00pages
748-58issue
3eissn
0300-9084issn
1638-6183pii
S0300-9084(11)00422-6journal_volume
94pub_type
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