Publications by authors named "D M Warshaw"
Article Synopsis
- Myosin-binding protein H (MyBP-H) is similar to MyBP-C and is found in skeletal muscle but has an unclear function, particularly in adult fast-twitch muscle.
- Research indicates that MyBP-H is highly expressed in prenatal rat fast-twitch muscles and larval zebrafish, hinting at its role in muscle development, which is being further investigated.
- While MyBP-H lacks key domains found in MyBP-C that modulate muscle contractility, experiments show it may function similarly by acting as a molecular "brake," raising new questions about muscle development roles.
Article Synopsis
- Kinesin-1 motors transport vesicles through a complex microtubule network, with research focusing on how these cargoes navigate intersections.
- Multiple kinesin motors engage a lipid-based cargo, but only a few (typically up to three) are actively working on it at any time.
- The study developed a mathematical model that explains the observed behaviors at 2D and 3D intersections, revealing a consistent mechanism for cargo navigation that is similar across different motor proteins like myosin Va.
Myosin-binding protein H (MyBP-H) is a component of the vertebrate skeletal muscle sarcomere with sequence and domain homology to myosin-binding protein C (MyBP-C). Whereas skeletal muscle isoforms of MyBP-C (fMyBP-C, sMyBP-C) modulate muscle contractility via interactions with actin thin filaments and myosin motors within the muscle sarcomere "C-zone," MyBP-H has no known function. This is in part due to MyBP-H having limited expression in adult fast-twitch muscle and no known involvement in muscle disease.
View Article and Find Full Text PDFDilated cardiomyopathy (DCM) is a condition characterized by impaired cardiac function, due to myocardial hypo-contractility, and is associated with point mutations in β-cardiac myosin, the molecular motor that powers cardiac contraction. Myocardial function can be modulated through sequestration of myosin motors into an auto-inhibited "super-relaxed" state (SRX), which may be further stabilized by a structural state known as the "interacting heads motif" (IHM). Here, we sought to determine whether hypo-contractility of DCM myocardium results from reduced function of individual myosin molecules or from decreased myosin availability to interact with actin due to increased IHM/SRX stabilization.
View Article and Find Full Text PDF