Prominin 1 and Tweety Homology 1 both induce extracellular vesicle formation.

Prominin 1 (Prom1) is a five-transmembrane pass integral membrane protein that associates with curved regions of the plasma membrane. Prom1 interacts with membrane cholesterol and actively remodels the plasma membrane. Membrane-bending activity is particularly evident in photoreceptors, where Prom1 loss-of-function mutations cause failure of outer segment homeostasis, leading to cone-rod retinal dystrophy (CRRD).

Reliability of muscle stiffness measures in popliteus, medial and lateral gastrocnemius muscles by ultrasound shear wave elastography in participants with knee osteoarthritis accompanied by myofascial trigger points.

Background: The objective of this investigation is to evaluate the consistency of intra-rater and inter-rater assessments utilizing ultrasound elastography to examine the muscle stiffness of the popliteus and gastrocnemius (medial and lateral heads) in patients with knee osteoarthritis accompanied by myofascial trigger points.

Methods: Thirty individuals with knee osteoarthritis accompanied by myofascial trigger points were assessed. Two examiners independently measured the muscle stiffness levels of the popliteus and gastrocnemius (medial and lateral heads) three times using ultrasound elastography in the first session.

Identification of SLC25A46 interaction interfaces with mitochondrial membrane fusogens Opa1 and Mfn2.

Mitochondrial fusion requires the sequential merger of four bilayers to two. The outer-membrane solute carrier protein SLC25A46 interacts with both the outer and inner-membrane dynamin family GTPases Mfn1/2 and Opa1. While SLC25A46 levels are known to affect mitochondrial morphology, how SLC25A46 interacts with Mfn1/2 and Opa1 to regulate membrane fusion is not understood.

In situ architecture of Opa1-dependent mitochondrial cristae remodeling.

Cristae membrane state plays a central role in regulating mitochondrial function and cellular metabolism. The protein Optic atrophy 1 (Opa1) is an important crista remodeler that exists as two forms in the mitochondrion, a membrane-anchored long form (l-Opa1) and a processed short form (s-Opa1). The mechanisms for how Opa1 influences cristae shape have remained unclear due to lack of native three-dimensional views of cristae.