Methods of Measuring Laryngeal Muscle Tension in Patients with Muscle Tension Dysphonia: A Scoping Review.

Background: In clinical practice and research relating to Muscle Tension Dysphonia (MTD), several laryngeal muscle tension measurement methods are used to diagnose, to identify specific muscle strengths and deficits, and to measure therapeutic outcomes. The variety and reliability of available measurement methods presents challenges within diagnosis and treatment. The lack of methodical standardization presents a barrier to homogeneous practice in this area.

Annexin B9 binds to β(H)-spectrin and is required for multivesicular body function in Drosophila.

The role of the cytoskeleton in protein trafficking is still being defined. Here, we describe a relationship between the small Ca(2+)-dependent membrane-binding protein Annexin B9 (AnxB9), apical β(Heavy)-spectrin (β(H)) and the multivesicular body (MVB) in Drosophila. AnxB9 binds to a subset of β(H) spliceoforms, and loss of AnxB9 results in an increase in basolateral β(H) and its appearance on cytoplasmic vesicles that overlap with the MVB markers Hrs, Vps16 and EPS15.

The cell adhesion molecule Roughest depends on beta(Heavy)-spectrin during eye morphogenesis in Drosophila.

Cell junctions have both structural and morphogenetic roles, and contain complex mixtures of proteins whose interdependencies are still largely unknown. Junctions are also major signaling centers that signify correct integration into a tissue, and modulate cell survival. During Drosophila eye development, the activity of the immunoglobulin cell adhesion molecule Roughest (also known as Irregular chiasm C-roughest protein) mediates interommatidial cell (IOC) reorganization, leading to an apoptotic event that refines the retinal lattice.

Brush border spectrin is required for early endosome recycling in Drosophila.

An apical brush border is a characteristic of many mature epithelia. This dynamic structure consists of dense microvilli supported by F-actin bundles that protrude into the apical cytoplasm, where they are crosslinked by spectrin and myosin II to form the terminal web. Little is known about the terminal web, through which vesicles transit to and from the apical membrane.

Styrylquinolines, integrase inhibitors acting prior to integration: a new mechanism of action for anti-integrase agents.

We have previously shown that styrylquinolines (SQLs) are integrase inhibitors in vitro. They compete with the long terminal repeat substrate for integrase. Here, we describe the cellular mode of action of these molecules.

The C-terminal domain of Drosophila (beta) heavy-spectrin exhibits autonomous membrane association and modulates membrane area.

Current models of cell polarity invoke asymmetric cues that reorganize the secretory apparatus to induce polarized protein delivery. An important step in this process is the stabilization of the protein composition in each polarized membrane domain. The spectrin-based membrane skeleton is thought to contribute to such stabilization by increasing the half-life of many proteins at the cell surface.

Crumbs interacts with moesin and beta(Heavy)-spectrin in the apical membrane skeleton of Drosophila.

The apical transmembrane protein Crumbs is necessary for both cell polarization and the assembly of the zonula adherens (ZA) in Drosophila epithelia. The apical spectrin-based membrane skeleton (SBMS) is a protein network that is essential for epithelial morphogenesis and ZA integrity, and exhibits close colocalization with Crumbs and the ZA in fly epithelia. These observations suggest that Crumbs may stabilize the ZA by recruiting the SBMS to the junctional region.

Apical spectrin is essential for epithelial morphogenesis but not apicobasal polarity in Drosophila.

Changes in cell shape and position drive morphogenesis in epithelia and depend on the polarized nature of its constituent cells. The spectrin-based membrane skeleton is thought to be a key player in the establishment and/or maintenance of cell shape and polarity. We report that apical beta(Heavy)-spectrin (beta(H)), a terminal web protein that is also associated with the zonula adherens, is essential for normal epithelial morphogenesis of the Drosophila follicle cell epithelium during oogenesis.