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Biology subjects

Rubio, M. A.

Publications and source records attributed to Rubio, M. A..

2 recordsLinked to original sources

The cyanobacterium Anabaena uses pleomorphism as an acclimation strategy to high light stress

O_LIPhytoplankton species display characteristic morphologies that are generally assumed to confer adaptive advantages, yet the functional significance of cell shape remains poorly understood. Here, we investigated whether pleomorphism contributes to acclimation to changing light environments. C_LIO_LIUsing the cyanobacterium Anabaena sp. PCC 7120 as a model system, we combined molecular genetics, microscopy, physiological measurements and biophysical analyses to determine how morphology is regulated and how it affects photosynthetic performance under different light intensities. C_LIO_LIWe show that Anabaena undergoes a reversible light-dependent morphological transition from rod-shaped cells under low light to large globular cells under high light stress. This transition is controlled by the relative activities of the elongasome and class A penicillin-binding proteins and is accompanied by thylakoid reorganization. The globular morphology reduces light absorption and enables cells to maintain photosynthetic activity under photoinhibitory conditions. C_LIO_LIOur findings establish a mechanistic link between cell-wall remodelling, cellular optics and photosynthetic performance, revealing pleomorphism as a dynamic acclimation strategy to high light stress. More broadly, this work provides experimental support for the packaging effect and highlights morphology as an active determinant of phytoplankton fitness. C_LI

plant biology↗

Combined thermodynamic and time-resolved structural analysis of interactions between AP2 and biomimetic plasma membranes provides insights into clathrin-mediated endocytosis

Clathrin mediated endocytosis (CME) is the main mechanism for swift and selective uptake of proteins into eukaryotic cells. CME is initiated by recruitment to the plasma membrane (PM) of the adaptor protein AP2, which recognizes the PM-associated lipid PtdIns(4,5)P2, as well as the protein cargo to be internalized. Nonetheless, many aspects of this process remain unclear due to their in vivo complexity. Here, a thermodynamic and time-resolved structural analysis of AP2 binding to different biomimetic PM was undertaken under physiological conditions using a combination of neutron reflectometry, interfacial tensiometry and rheology, and atomic force microscopy. The resultant in vitro data replicated previous in vivo observations, as well as yielded biophysical insights into normal and aborted CME. The presence of cargo may not be pivotal for the "activating" conformational change of AP2. However, the presence of cargo extends AP2s residence time on the membrane surface, due to slower on- and off-rates, thereby tentatively giving sufficient time for CME to proceed fully. Moreover, upon interaction with AP2, phospholipid lateral diffusion decreases markedly, inducing a gel phase attributed to creating a percolated network involving AP2 on the membrane, which could potentially serve as a mechanism for modulating subsequent clathrin binding.

biophysics↗