Peroxisomes carry out various oxidative reactions that are tightly regulated to adapt to the changing needs of the cell and varying external environments. Accordingly, they are remarkably fluid and can change dramatically in abundance, size, shape and content in response to numerous cues. These dynamics are controlled by multiple aspects of peroxisome biogenesis that are coordinately regulated with each other and with other cellular processes. Ongoing studies are deciphering the diverse molecular mechanisms that underlie biogenesis and how they cooperate to dynamically control peroxisome utility. These important challenges should lead to an understanding of peroxisome dynamics that can be capitalized upon for bioengineering and the development of therapies to improve human health.

Peroxisomes take shape

Lipid droplets (LDs) and peroxisomes are central players in cellular lipid homeostasis: some of their main functions are to control the metabolic flux and availability of fatty acids (LDs and peroxisomes) as well as of sterols (LDs). Both fatty acids and sterols serve multiple functions in the cell—as membrane stabilizers affecting membrane fluidity, as crucial structural elements of membrane-forming phospholipids and sphingolipids, as protein modifiers and signaling molecules, and last but not least, as a rich carbon and energy source. In addition, peroxisomes harbor enzymes of the malic acid shunt, which is indispensable to regenerate oxaloacetate for gluconeogenesis, thus allowing yeast cells to generate sugars from fatty acids or nonfermentable carbon sources. Therefore, failure of LD and peroxisome biogenesis and function are likely to lead to deregulated lipid fluxes and disrupted energy homeostasis with detrimental consequences for the cell. These pathological consequences of LD and peroxisome failure have indeed sparked great biomedical interest in understanding the biogenesis of these organelles, their functional roles in lipid homeostasis, interaction with cellular metabolism and other organelles, as well as their regulation, turnover, and inheritance. These questions are particularly burning in view of the pandemic development of lipid-associated disorders worldwide.

https://www.genetics.org/content/genetics/193/1/1.full.pdf

Lipid Droplets and Peroxisomes: Key Players in Cellular Lipid Homeostasis or A Matter of Fat-Store 'em Up or Burn 'em Down

In Channelrhodopsin-2 Glu-90 Is Crucial for Ion Selectivity and Is Deprotonated during the Photocycle

http://labs.biology.ucsd.edu/subramani/documents/Liu_Ma_Suresh1.pdf

Recent advances in peroxisomal matrix protein import.

The class A G-protein-coupled receptors (GPCRs) Orexin-1 (OX1) and Orexin-2 (OX2) are located predominantly in the brain and are linked to a range of different physiological functions, including the control of feeding, energy metabolism, modulation of neuro-endocrine function, and regulation of the sleep–wake cycle Site-directed mutagenesis (SDM) and domain exchange (chimera) studies have provided important insight into key features of the OX1 and OX2 binding sites However, the precise determinants of antagonist binding and selectivity are still not fully known In this work, we used homology modeling of OX receptors to direct further SDM studies These SDM studies were followed by molecular dynamics (MD) simulations to rationalize the full scope of the SDM data and to explain the role of each mutated residue in the binding and selectivity of a set of OX antagonists: Almorexant (dual OX1 and OX2 antagonist), SB-674042 (OX1 selective antagonist), EMPA (OX2 selective antagonist), and others Our primary i

Study of human Orexin-1 and -2 G-protein-coupled receptors with novel and published antagonists by modeling, molecular dynamics simulations, and site-directed mutagenesis.

Identification of PEX33, a novel component of the peroxisomal docking complex in the filamentous fungus Neurospora crassa.

http://www.robotics.tu-berlin.de/fileadmin/fg170/Publikationen_pdf/Schneider%20et%20al.%20-%202011%20-%20The%20structure%20of%20active%20opsin%20as%20a%20basis%20for%20ident.pdf

The structure of active opsin as a basis for identification of GPCR agonists by dynamic homology modelling and virtual screening assays.

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Identification of PEX33, a novel component of the peroxisomal docking complex in the filamentous fungus Neurospora crassa.

The structure of active opsin as a basis for identification of GPCR agonists by dynamic homology modelling and virtual screening assays.