Cellular Signaling and Protein Phosphorylation

<p>It serves as a signal for regulating downstream signaling events. (A)</p> Signup and view all the answers

<p>It can form repeated regions within the same polypeptide or across different proteins. (B)</p> Signup and view all the answers

<p>To catalyze phosphorylation of protein substrates (B)</p> Signup and view all the answers

<p>SH2, SH3, and PTB domains (C)</p> Signup and view all the answers

<p>It functions as a dual-specificity protein phosphatase (B)</p> Signup and view all the answers

<p>It interacts with the phospho tyrosine of RTKs through its SH2 domain. (B)</p> Signup and view all the answers

<p>PH domains (C)</p> Signup and view all the answers

<p>They bind specifically to motifs containing a phosphotyrosine. (A)</p> Signup and view all the answers

<p>Structural interaction domains (C)</p> Signup and view all the answers

<p>Receptor tyrosine kinases and non-RTKs (A)</p> Signup and view all the answers

<p>Anchor transmembrane proteins to the cytoskeleton (B)</p> Signup and view all the answers

<p>EF-hand motif (D)</p> Signup and view all the answers

<p>Post synaptic density protein (C)</p> Signup and view all the answers

<p>Protein kinase domains (C)</p> Signup and view all the answers

<p>Coupling of receptor to Gq (B)</p> Signup and view all the answers

<p>Retardation of visual resolution (B)</p> Signup and view all the answers

<p>C2 domain (D)</p> Signup and view all the answers

<p>To facilitate calcium release (A)</p> Signup and view all the answers

<p>To recognize and bind a PDZ domain on other signaling molecules (C)</p> Signup and view all the answers

<p>They enhance the efficiency and/or specificity of cellular pathways (D)</p> Signup and view all the answers

<p>Contain an active guanylate kinase domain (A)</p> Signup and view all the answers

<p>Phototransduction cascade proteins (B)</p> Signup and view all the answers

<p>Through peptide interactions recognizing specific sequences (D)</p> Signup and view all the answers

<p>PDZ domain, SH3 domain, and GUK domain (C)</p> Signup and view all the answers

<p>NHERF (C)</p> Signup and view all the answers

<p>They generally consist of 8–10 residues of Pro. (A)</p> Signup and view all the answers

<p>PDZ-based scaffold proteins can interact with a diverse range of signaling partners. (A)</p> Signup and view all the answers

<p>Adaptor proteins such as Grb2 and Nck. (C)</p> Signup and view all the answers

<p>PTB domain. (D)</p> Signup and view all the answers

<p>They play a role in protein–protein interactions. (A)</p> Signup and view all the answers

<p>They are involved in regulating cellular processes. (B)</p> Signup and view all the answers

<p>To recognize sequences distinctly from phoshotyrosine motifs. (B)</p> Signup and view all the answers

<p>Phosphoinositides. (A)</p> Signup and view all the answers

<p>They possess a hydrophobic binding surface. (C)</p> Signup and view all the answers

<p>Calcium binding (B)</p> Signup and view all the answers

<p>PH domain (D)</p> Signup and view all the answers

<p>SH2 and SH3 domains (A)</p> Signup and view all the answers

<p>Beta-sandwich structure (A)</p> Signup and view all the answers

<p>Calcium (A)</p> Signup and view all the answers

<p>Involves a helix-loop-helix structure (A)</p> Signup and view all the answers

<p>Two cysteines and two histidines (C)</p> Signup and view all the answers

<p>Antiparallel beta strands (C)</p> Signup and view all the answers

Specific regions within proteins that actively participate in recognition processes.

A common way for cells to transmit information by adding a phosphate group to a protein.

An enzyme that adds a phosphate group to a protein.

Regions within proteins with a specific 3D structure and function.

Domains that bind to phosphorylated tyrosine residues.

Transmembrane proteins with intrinsic tyrosine kinase activity. They play a crucial role in signal transduction by phosphorylating tyrosine residues on target proteins, including themselves.

The catalytic domain of RTKs located in the cytoplasm. It is responsible for phosphorylating tyrosine residues on target proteins, initiating signal transduction pathways.

A dual-specificity protein phosphatase that removes phosphate groups from tyrosine, serine, and threonine residues on proteins. It plays a crucial role in regulating cell growth and survival.

Phosphatidyl inositol (4,5) biphosphate, a lipid molecule present in cell membranes. It serves as a substrate for enzymes like phospholipase C and PI3K.

Phosphatidyl inositol (3,4,5) triphosphate, a lipid molecule generated from PIP2 by PI3K. It acts as a second messenger in various signaling pathways.

Specialized regions within proteins that facilitate interactions with other proteins. They bind to specific peptide motifs or structural elements, enabling protein-protein interactions.

A protein interaction domain that binds to phosphorylated tyrosine residues (pTyr) on proteins. It plays a crucial role in mediating protein-protein interactions in signaling pathways.

A protein interaction domain that recognizes and binds to proline-rich motifs on proteins. It plays a key role in scaffolding proteins and signaling complexes.

Short sequences of amino acids within proteins that are rich in proline residues. They are often recognized by SH3 domains.

Domains that bind to phosphotyrosine residues (N-P-X-pY) but recognize distinct sequences compared to SH2 domains. They can also bind to acidic phospholipid head groups.

Seven main phosphoinositides are found in membranes of organelles and plasma membrane.

The major protein domains that bind to oligopeptide motifs are SH2, SH3, and PTB domains.

Phosphoinositide-binding motifs and domains, such as PH domains, help regulate protein localization to membranes.

A helix-loop-helix structure that binds calcium ions. Two EF-hand motifs often pair together to form a functional unit.

A calcium-binding protein with multiple EF-hand motifs. It acts as a calcium sensor, triggering downstream signaling pathways.

A protein domain containing a zinc ion coordinated by two cysteines and two histidines. This structure aids in DNA binding and recognition.

The PH domain of some proteins, such as GRK2, can bind to IP3 (inositol triphosphate).

PLCγ1 uses its PH domain to bind to PIP3, which is a lipid found in the cell membrane.

Major families include domains that bind oligopeptide motifs (SH2, SH3, PTB), phosphoinositide-binding motifs (PH), calcium-binding domains (EF-hand, C2), zinc finger domains (C2H2), protein kinase domains, and PDZ domains.

A short sequence of amino acids within a protein that specifically binds to a PDZ domain on another protein.

A PDZ binding motif interacts with a PDZ domain on another protein.

Proteins that act as organizing centres by binding to multiple other proteins, bringing them together to enhance signaling pathways.

Scaffold proteins can be PDZ-based or non-PDZ-based.

Scaffold proteins that have PDZ, SH3, and guanylate kinase (GUK) domains, involved in membrane-associated signaling pathways.

MAGUK proteins contain PDZ, SH3, and guanylate kinase (GUK) domains.

A scaffold protein involved in the fly phototransduction cascade, helps organize the signaling proteins.

A series of steps involving light, rhodopsin, Gq, PLCβ, DAG, Ca2+, TRP channels, and phosphorylation by PKC, leading to membrane depolarization and visual signal transduction in Drosophila photoreceptor cells.

A light-sensitive receptor protein in photoreceptor cells, which initiates the visual transduction pathway by activating Gq upon light absorption.

A G protein that couples to rhodopsin and activates PLCβ in the visual transduction pathway.

An enzyme that hydrolyzes PIP2 into DAG and IP3, generating signaling molecules that trigger Ca2+ release and further downstream events in the visual transduction pathway.

Transient receptor potential (TRP) channels are ion channels in photoreceptor cells that open in response to Ca2+ release, leading to membrane depolarization and signal transduction.