Publications by authors named "Hana Kimura"
Article Synopsis
- - The text discusses how during the early phase of infection, certain effectors help merge vesicles from the endoplasmic reticulum (ER) with a vacuole that harbors bacteria, transforming it into a compartment conducive to bacterial growth.
- - It highlights the effector protein DrrA's role in activating Rab1, albeit the mechanism of how DrrA facilitates the attachment of host vesicles to the vacuole remains uncertain.
- - Research reveals that exocyst components (Sec5, Sec15, Sec6) are essential for DrrA's function in recruiting ER-derived vesicles to the bacteria-containing vacuole, with Rab1 activation also being critical for this process.
PGAM5, a mitochondrial protein phosphatase that is genetically and biochemically linked to PINK1, facilitates mitochondrial division by dephosphorylating the mitochondrial fission factor Drp1. At the onset of mitophagy, PGAM5 is cleaved by PARL, a rhomboid protease that degrades PINK1 in healthy cells, and the cleaved form facilitates the engulfment of damaged mitochondria by autophagosomes by dephosphorylating the mitophagy receptor FUNDC1. Here, we show that the function and localization of PGAM5 are regulated by syntaxin 17 (Stx17), a mitochondria-associated membrane/mitochondria protein implicated in mitochondrial dynamics in fed cells and autophagy in starved cells.
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- Stx17 is a protein that helps regulate mitochondrial fission by interacting with Drp1 at the endoplasmic reticulum-mitochondria interface in fed cells.
- When cells are starved, Stx17 changes its interactions by leaving microtubules and Drp1 to bind with Atg14L, aiding in the formation of autophagosomes, which are essential for cellular recycling.
- The study identifies MAP1B-LC1 as a key player that connects Stx17 and microtubules, and its dephosphorylation during starvation allows Stx17 to switch partners for autophagosome formation.
Article Synopsis
- * The study highlights that syntaxin 17 (Stx17), a protein influenced by diet, plays a crucial role in LD formation by helping the enzyme acyl-CoA synthetase (ACSL)3 move from the endoplasmic reticulum (ER) to LDs.
- * Stx17 interacts specifically with ACSL3, enhancing its redistribution to LDs, and its absence can hinder LD maturation, but this can be offset by increasing ACSL3 levels, signaling the importance of this protein-protein
Article Synopsis
- - The yeast Dsl1 complex, made up of Dsl1, Tip20, and Sec39/Dsl3, helps in retrograde transport of materials from the Golgi apparatus back to the endoplasmic reticulum.
- - The metazoan NRZ complex, consisting of NAG, RINT1, and ZW10, similarly facilitates Golgi-to-ER transport but also plays various roles in processes like endosome-to-Golgi transport, cytokinesis, and mRNA decay.
- - The review highlights the multiple functions of the NRZ complex components and examines how they interact with each other beyond their main roles in trafficking.
Article Synopsis
- The morphology and distribution of the endoplasmic reticulum (ER) in mammalian cells are influenced by how ER membrane proteins interact with microtubules (MTs).
- The protein CLIMP-63 is important for maintaining the structure of rough ER and its static connection with MTs, while the syntaxin 5 variant Syn5L also plays a role by interacting with both CLIMP-63 and MTs.
- New findings reveal that VIMP, another protein, influences ER structure and distribution by interacting with MTs, but does not connect with all MT-binding proteins, indicating that various proteins are involved in organizing different ER regions.