Other Substrates

Paxillin (Tyr 181) is a pivotal adaptor protein that plays a significant role in cellular signaling and structural integrity. Phosphorylation at Tyr 181 enhances its interaction with other proteins, particularly in the context of focal adhesion dynamics. This modification influences the recruitment of signaling complexes, thereby impacting pathways related to cell shape and movement. Additionally, it contributes to the regulation of integrin signaling, highlighting its importance in mechanosensing and cellular response to environmental cues.

Phospholamban (Thr 17) is a crucial regulatory protein that modulates calcium handling in cardiac muscle cells. Phosphorylation at Thr 17 alters its conformation, enhancing its interaction with the sarcoplasmic reticulum calcium ATPase (SERCA). This modification accelerates calcium reuptake, influencing cardiac contractility and relaxation. The dynamic interplay between phospholamban and SERCA is vital for maintaining calcium homeostasis, impacting cardiac function and rhythm.

PI 3-kinase p85α (Tyr 508) serves as a pivotal adaptor protein in cellular signaling pathways, particularly in the regulation of lipid metabolism and cell growth. The phosphorylation at Tyr 508 enhances its binding affinity to p110 catalytic subunits, facilitating the activation of phosphoinositide 3-kinase (PI3K) signaling. This interaction is crucial for downstream effects on Akt signaling, influencing cellular responses to growth factors and stress. Its role in modulating these pathways underscores its importance in cellular homeostasis and metabolic regulation.

PKC δ (Thr 507) is a serine/threonine kinase that is pivotal in regulating cellular responses to oxidative stress and inflammation. Phosphorylation at Thr 507 modulates its activity, facilitating interactions with distinct substrates that influence various signaling pathways. This modification can enhance the kinase's ability to phosphorylate target proteins, thereby affecting cellular processes such as migration and survival. The unique conformational changes induced by this phosphorylation also impact its localization and interaction with other signaling molecules.

PKC ε (Ser 729) is a serine/threonine kinase that plays a critical role in various signaling cascades, particularly in response to stress and growth factors. Phosphorylation at Ser 729 enhances its enzymatic activity and promotes interactions with specific substrates, influencing downstream signaling pathways. This modification can alter cellular dynamics, including apoptosis and differentiation, by modulating protein-protein interactions and affecting the localization of signaling complexes within the cell.

PKR (Thr 446) is a key player in cellular signaling, particularly in response to stress stimuli. The phosphorylation at Thr 446 enhances its affinity for specific substrates, leading to distinct downstream effects. This modification alters the enzyme's conformation, promoting unique interactions that can modulate various signaling cascades. Additionally, PKR's kinetic properties allow for rapid activation and deactivation, enabling precise control over cellular responses to environmental changes.

PKR (Thr 451) exhibits unique characteristics as an acid halide, particularly in its reactivity with nucleophiles. The presence of the halogen enhances electrophilicity, facilitating rapid acylation reactions. Its distinct steric and electronic properties influence reaction kinetics, allowing for selective substrate interactions. Furthermore, PKR's ability to form stable intermediates contributes to its role in various synthetic pathways, showcasing its versatility in chemical transformations.

Plasminogen (Ser 578) is notable for its role in the fibrinolytic pathway, where it undergoes conversion to plasmin. This transformation is facilitated by specific proteolytic enzymes, highlighting its unique molecular interactions. The presence of serine at position 578 plays a critical role in substrate specificity and binding affinity. Additionally, plasminogen's conformational flexibility allows it to interact with various proteins, influencing its activation kinetics and downstream effects in cellular processes.

PP2A (Tyr 307) is a pivotal serine/threonine phosphatase involved in diverse signaling pathways. Its unique interaction with regulatory subunits modulates substrate specificity, influencing cellular processes such as cell growth and apoptosis. The phosphorylation state at Tyr 307 is crucial for its activity, affecting the enzyme's conformation and stability. This dynamic regulation allows PP2A to participate in intricate feedback loops, impacting various cellular responses and maintaining homeostasis.

PRK2 (Thr 816) is a serine/threonine kinase that plays a critical role in cellular signaling networks. Its phosphorylation at Thr 816 enhances substrate affinity and alters interaction dynamics with downstream effectors. This modification influences various pathways, including stress response and cell migration. The enzyme exhibits distinct reaction kinetics, characterized by rapid activation and a unique regulatory mechanism that fine-tunes its activity in response to cellular stimuli.