GABA release by hippocampal astrocytes

10 p.

Entrevista a Alfonso Zapico

Entrevista realizada al historietista asturiano Alfonso Zapico

Transformaciones en el retablo mayor de San Miguel Arcángel de Lazkao (Gipuzkoa): del Barroco al Neoclasicismo

[ES] El retablo mayor de la localidad guipuzcoana de Lazkao fue realizado por Juan de Ursularre en 1683, siguiendo los parámetros de la retablística barroca. Queriendo engrandecer su aspecto, fue paulatinamente transformado durante el siglo XVIII. Por ello se concibió un nuevo cascarón con pinturas enviadas desde Madrid y más tarde se adecuó a los nuevos gustos neoclásicos mediante una radical reforma realizada en 1791 que consistió en eliminar todo atisbo de decoración barroca.

Specific Interaction with Cardiolipin Triggers Functional Activation of Dynamin-Related Protein 1

Dynamin-Related Protein 1 (Drp1), a large GTPase of the dynamin superfamily, is required for mitochondrial fission in healthy and apoptotic cells. Drp1 activation is a complex process that involves translocation from the cytosol to the mitochondrial outer membrane (MOM) and assembly into rings/spirals at the MOM, leading to membrane constriction/division. Similar to dynamins, Drp1 contains GTPase (G), bundle signaling element (BSE) and stalk domains. However, instead of the lipid-interacting Pleckstrin Homology (PH) domain present in the dynamins, Drp1 contains the so-called B insert or variable domain that has been suggested to play an important role in Drp1 regulation. Different proteins have been implicated in Drp1 recruitment to the MOM, although how MOM-localized Drp1 acquires its fully functional status remains poorly understood. We found that Drp1 can interact with pure lipid bilayers enriched in the mitochondrion-specific phospholipid cardiolipin (CL). Building on our previous study, we now explore the specificity and functional consequences of this interaction. We show that a four lysine module located within the B insert of Drp1 interacts preferentially with CL over other anionic lipids. This interaction dramatically enhances Drp1 oligomerization and assembly-stimulated GTP hydrolysis. Our results add significantly to a growing body of evidence indicating that CL is an important regulator of many essential mitochondrial functions.