☆ 4.6 Article

Insulin receptor Arg717 and IGF-1 receptor Arg704 play a key role in ligand binding and in receptor activation

OPEN BIOLOGY (2023)

Related references

Note: Only part of the references are listed.

Review Biochemistry & Molecular Biology

The Activation Mechanism of the Insulin Receptor: A Structural Perspective

Eunhee Choi et al.

Summary: The insulin receptor (IR) is a type II receptor tyrosine kinase that plays crucial roles in metabolism, growth, and proliferation. Recent advances in cryo-electron microscopy have allowed the determination of IR structures with different numbers of bound insulin molecules, providing important insights into the activation mechanism of this receptor. This review summarizes the insulin-induced activation mechanism of IR, including the binding modes and functions of insulin at different sites, as well as the structural transitions necessary for IR activation. It also highlights key aspects of IR signaling activation and regulation and suggests future research directions to fill the remaining gaps in our understanding.

ANNUAL REVIEW OF BIOCHEMISTRY (2023)

Add to Collection

Article Medicine, Research & Experimental

Leucine-973 is a crucial residue differentiating insulin and IGF-1 receptor signaling

Hirofumi Nagao et al.

Summary: Insulin and IGF-1 receptors have similar signaling systems but different physiological roles. Replacement of leucine-973 in the intracellular juxtamembrane region with phenylalanine resulted in altered signaling, decreased insulin sensitivity, increased cell growth, and impaired receptor internalization. This amino acid residue plays a crucial role in differentiating the signaling of IR and IGF1R.

JOURNAL OF CLINICAL INVESTIGATION (2023)

Add to Collection

Article Biochemistry & Molecular Biology

Insulin receptor Arg717 and IGF-1 receptor Arg704 play a key role in ligand binding and in receptor activation

Anna Kertisova et al.

Summary: This study investigates the transition between inactive and active states of insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF-1R) through mutation of key residues. The results show that these mutations significantly affect the binding and activation abilities of the receptors, providing further insights into the relationship between the structure and function of these receptors.

OPEN BIOLOGY (2023)

Add to Collection

Article Biochemistry & Molecular Biology

Structural Investigations of Full-Length Insulin Receptor Dynamics and Signalling

Jeppe Nielsen et al.

Summary: Insulin regulates glucose homeostasis by binding and activating the insulin receptor in an asymmetric manner. This study reveals how insulin binds at two distinct sites and disrupts the autoinhibited state, stabilizing the active state of the receptor.

JOURNAL OF MOLECULAR BIOLOGY (2022)

Add to Collection

Article Biochemistry & Molecular Biology

Synergistic activation of the insulin receptor via two distinct sites

Jie Li et al.

Summary: This study reveals the effect of insulin binding on the conformation and activation of the insulin receptor (IR), demonstrating how the synergistic binding of multiple insulins promotes optimal IR activation.

NATURE STRUCTURAL & MOLECULAR BIOLOGY (2022)

Add to Collection

Article Biochemistry & Molecular Biology

How insulin-like growth factor I binds to a hybrid insulin receptor type 1 insulin-like growth factor receptor

Yibin Xu et al.

Summary: Monomers of the insulin receptor and type 1 insulin-like growth factor receptor can form heterodimeric hybrid receptors, which display different ligand binding and signaling properties from homodimeric receptors. Cryoelectron microscopy structure reveals that the hybrid receptor binds insulin-like growth factor I in a similar fashion to IGF-1R, involving specific structural motifs. This study expands our understanding of this receptor family and provides insights into the key structural determinants involved in ligand binding.

STRUCTURE (2022)

Add to Collection

Article Multidisciplinary Sciences

Interaction of a viral insulin-like peptide with the IGF-1 receptor produces a natural antagonist

Francois Moreau et al.

Summary: This study identifies a viral insulin/IGF-1 like peptide (VILP) with antagonist properties on IGF-1 receptor signaling, leading to inhibition of cell proliferation and growth. Cryo-electron microscopy reveals that this VILP engages with IGF1R in a unique manner, resulting in receptor inactivation.

NATURE COMMUNICATIONS (2022)

Add to Collection

Article Biology

Molecular basis for the role of disulfide-linked aCTs in the activation of insulin-like growth factor 1 receptor and insulin receptor

Jie Li et al.

Summary: The insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R) play crucial roles in metabolic homeostasis and cell growth. This study reveals that the structural rigidity of the disulfide-linked alpha CTs is critical for optimal IR and IGF1R signaling activation.

ELIFE (2022)

Add to Collection

Review Biochemistry & Molecular Biology

Mini Review: Molecular Interpretation of the IGF/IGF-1R Axis in Cancer Treatment and Stem Cells-Based Therapy in Regenerative Medicine

Syuan-Ling Lin et al.

Summary: This review focuses on the role of IGF/IGF-1R signaling in cancer initiation and proliferation, maintenance of stem cell characteristics, and enhancement of stem cell-based therapeutics. It summarizes the current progress in preclinical IGF-targeted therapies and the function of IGF/IGF-1R signaling in stem cell self-renewal and regenerative medicine.

INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES (2022)

Add to Collection

Article Biochemistry & Molecular Biology

Cryo-EM structure shows how two IGF1 hormones bind to the human IGF1R receptor

Cang Wu et al.

Summary: This study reports a new cryo-EM structure of IGF1R, which resolves the controversy regarding its binding mechanism and proposes a new theory for ligand binding.

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS (2022)

Add to Collection

Review Biochemistry & Molecular Biology

Recent developments in the structural characterisation of the IR and IGF1R: implications for the design of IR-IGF1R hybrid receptor modulators

Samuel J. Turvey et al.

Summary: This review discusses the advances in structural understanding of the insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R) and the importance of designing small-molecule modulators to study the role of IR-IGF1R hybrid receptors in cell biology.

RSC MEDICINAL CHEMISTRY (2022)

Add to Collection

Article Multidisciplinary Sciences

Continuous variable responses and signal gating form kinetic bases for pulsatile insulin signaling and emergence of resistance

Namrata Shukla et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2021)

Add to Collection

Article Multidisciplinary Sciences

Distinct signaling by insulin and IGF-1 receptors and their extra- and intracellular domains

Hirofumi Nagao et al.

Summary: Insulin receptor (IR) and insulin-like growth factor 1 receptor (IGF1R) show distinct downstream signaling pathways and biological effects, preferentially stimulating different phosphorylation networks such as mTORC1 and Akt pathways for IR and Rho GTPases for IGF1R. Despite their high homology, IR and IGF1R exhibit unique effects on organismal function through regulating distinct phosphoproteomes in both basal and stimulated states.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2021)

Add to Collection

Review Endocrinology & Metabolism

Understanding insulin and its receptor from their three-dimensional structures

Michael C. Lawrence

Summary: The article describes the three-dimensional structure of insulin and its receptor, as well as their interactions, highlighting research gaps in structural understanding. A near-complete picture has been obtained of hormone receptor interactions, providing new insights and requiring revision of the existing hormone receptor engagement models.

MOLECULAR METABOLISM (2021)

Add to Collection

Article Biochemical Research Methods

A radioligand receptor binding assay for measuring of insulin secreted by MIN6 cells after stimulation with glucose, arginine, ornithine, dopamine, and serotonin

Seiya Asai et al.

Summary: The study utilized an IR binding assay to determine insulin levels, showing comparable results to RIA kits. Arginine stimulated glucose-induced insulin secretion in MIN6 cells, while dopamine had inhibitory effects. The effects of serotonin varied with concentration levels. The IR binding assay allows for higher throughput and broader range of measurements compared to RIA kits.

ANALYTICAL AND BIOANALYTICAL CHEMISTRY (2021)

Add to Collection

Article Cell Biology

Cryo-EM structure of the complete and ligand-saturated insulin receptor ectodomain

Theresia Gutmann et al.

JOURNAL OF CELL BIOLOGY (2020)

Add to Collection

Article Biochemistry & Molecular Biology

Visualization of Ligand-Bound Ectodomain Assembly in the Full-Length Human IGF-1 Receptor by Cryo-EM Single-Particle Analysis

Xi Zhang et al.

STRUCTURE (2020)

Add to Collection

Article Biochemistry & Molecular Biology

How IGF-II Binds to the Human Type 1 Insulin-like Growth Factor Receptor

Yibin Xu et al.

STRUCTURE (2020)

Add to Collection

Article Multidisciplinary Sciences

A radioligand binding assay for the insulin-like growth factor 2 receptor

Pavlo Potalitsyn et al.

PLOS ONE (2020)

Add to Collection

Article Biology

Activation mechanism of the insulin receptor revealed by cryo-EM structure of the fully liganded receptor-ligand complex

Emiko Uchikawa et al.

ELIFE (2019)

Add to Collection

Article Biochemistry & Molecular Biology

Mutations at hypothetical binding site 2 in insulin and insulin-like growth factors 1 and 2 result in receptor- and hormone-specific responses

Katerina Machackova et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2019)

Add to Collection

Article Multidisciplinary Sciences

Structural basis of the activation of type 1 insulin-like growth factor receptor

Jie Li et al.

NATURE COMMUNICATIONS (2019)

Add to Collection

Article Chemistry, Physical

Tris-(Nitrilotriacetic Acid)-Decorated Polymer Conjugates as Tools for Immobilization and Visualization of His-Tagged Proteins

Jana Beranova et al.

CATALYSTS (2019)

Add to Collection

Article Cell Biology

Visualization of ligand-induced transmembrane signaling in the full-length human insulin receptor

Theresia Gutmann et al.

JOURNAL OF CELL BIOLOGY (2018)

Add to Collection

Article Multidisciplinary Sciences

How ligand binds to the type 1 insulin-like growth factor receptor

Yibin Xu et al.

NATURE COMMUNICATIONS (2018)

Add to Collection

Article Biochemistry & Molecular Biology

A versatile insulin analog with high potency for both insulin and insulin-like growth factor 1 receptors: Structural implications for receptor binding

Martina Chrudinova et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2018)

Add to Collection

Article Multidisciplinary Sciences

The signalling conformation of the insulin receptor ectodomain

Felix Weis et al.

NATURE COMMUNICATIONS (2018)

Add to Collection

Review Endocrinology & Metabolism

Insulin Receptor Isoforms in Physiology and Disease: An Updated View

Antonino Belfiore et al.

ENDOCRINE REVIEWS (2017)

Add to Collection

Article Chemistry, Medicinal

Insulin-like Growth Factor 1 Analogs Clicked in the C Domain: Chemical Synthesis and Biological Activities

Katerina Machackova et al.

JOURNAL OF MEDICINAL CHEMISTRY (2017)

Add to Collection

Article Biochemistry & Molecular Biology

Insulin-Insulin-like Growth Factors Hybrids as Molecular Probes of Hormone:Receptor Binding Specificity

Kvetoslava Krizkova et al.

BIOCHEMISTRY (2016)

Add to Collection

Article Biochemistry & Molecular Biology

Insulin/receptor binding: The last piece of the puzzle?

Pierre De Meyts

BIOESSAYS (2015)

Add to Collection

Article Multidisciplinary Sciences

How insulin engages its primary binding site on the insulin receptor

John G. Menting et al.

NATURE (2013)

Add to Collection

Article Biochemistry & Molecular Biology

Insight into the molecular basis for the kinetic differences between the two insulin receptor isoforms

Louise Knudsen et al.

BIOCHEMICAL JOURNAL (2011)

Add to Collection

Article Endocrinology & Metabolism

Insulin analogues differently activate insulin receptor isoforms and post-receptor signalling

L. Sciacca et al.

DIABETOLOGIA (2010)

Add to Collection

Article Biochemistry & Molecular Biology

Harmonic oscillator model of the insulin and IGF1 receptors' allosteric binding and activation

Vladislav V. Kiselyov et al.

MOLECULAR SYSTEMS BIOLOGY (2009)

Add to Collection

Article Biochemistry & Molecular Biology

High-Affinity Insulin Binding: Insulin Interacts with Two Receptor Ligand Binding Sites

Linda Whittaker et al.

BIOCHEMISTRY (2008)

Add to Collection

Article Biochemistry & Molecular Biology

Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I

Lisbeth Gauguin et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2008)

Add to Collection

Article Biochemistry & Molecular Biology

An investigation of the ligand binding properties and negative cooperativity of soluble insulin-like growth factor receptors

Katharina Helen Surinya et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2008)

Add to Collection

Article Multidisciplinary Sciences

Structure of the insulin receptor ectodomain reveals a folded-over conformation

Neil M. McKern et al.

NATURE (2006)

Add to Collection

Article Biochemistry & Molecular Biology

Characterization of the functional insulin binding epitopes of the full-length insulin receptor

J Whittaker et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2005)

Add to Collection

Article Biotechnology & Applied Microbiology

Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp red fluorescent protein

NC Shaner et al.

NATURE BIOTECHNOLOGY (2004)

Add to Collection

Article Biochemistry & Molecular Biology

Alanine scanning mutagenesis of a type 1 insulin-like growth factor receptor ligand binding site

J Whittaker et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2001)

Add to Collection

© Peeref 2019-2024. All rights reserved.