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Receptor Tyrosine Kinases Overview

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Questions and Answers

What defines Receptor Tyrosine Kinases (RTKs)?

Presence of serine kinase activity

Presence of tyrosine kinase activity (correct)

Presence of G protein activity

Presence of lipid kinase activity

How do RTKs behave in their monomeric form?

They contain multiple subunits

They are inactive (correct)

They exist as dimers of two hemireceptors

They dimerize upon ligand binding

What happens to RTKs when they bind one ligand molecule?

They dissociate

They heterodimerize with closely related receptors

They dimerize (correct)

They remain monomeric

Which receptors are an exception to the typical dimerization pattern of RTKs?

Insulin and IGF-1 receptors Signup and view all the answers

What binds to the N-terminal extracellular ligand binding domains of RTKs?

One molecule of ligand Signup and view all the answers

How many receptor tyrosine kinases are encoded in the human genome?

58 Signup and view all the answers

What distinguishes the carboxy terminals of RTKs like insulin/IGF-1 receptors and FGFR from others?

Insertion of non-TK amino acids Signup and view all the answers

What is a characteristic feature of the nuclear receptors?

They form heterodimers with RXR to bind DNA sequences Signup and view all the answers

How do receptors for cortisol and aldosterone behave prior to ligand binding?

They are bound to chaperone proteins in the cytoplasm Signup and view all the answers

What is the function of the N-terminal sequence in nuclear receptors?

It regulates gene transcription independently of ligand binding Signup and view all the answers

How are the receptors for thyroid hormone and 1α,25(OH)2-vitamin D3 typically found in target cells?

Bound to chaperone proteins in the nucleus Signup and view all the answers

What distinguishes about half of the nuclear receptors according to the text?

Activity-modulating ligands have not been identified for them Signup and view all the answers