Our Research

Iyer Lab

The Role of ER Sensor Proteins and Unfolded Protein Response (UPR):

The health of the endoplasmic reticulum (ER) is monitored by a triad of ER sensor transmembrane proteins: ATF6, Ire1a, and Perk. Accumulation of misfolded proteins in the ER leads to ER stress, activating these sensor proteins and initiating the Unfolded Protein Response (UPR) to restore homeostasis. However, if protein folding remains unresolved, elevated UPR can stimulate cytokine production and cell death.

Exploring ER-Associated Degradation (ERAD) and Misfolded Protein Clearance: Another critical aspect of ER homeostasis is ER-associated degradation (ERAD), a retrograde pathway responsible for recognizing and clearing misfolded proteins from the ER.

Role of UPR Genes in Skeletal Health and Pathology: In the Iyer Lab, we utilize mouse models to investigate the role of UPR genes in osteoblast lineage cells. By deleting specific UPR genes, we aim to understand the mechanisms by which the UPR regulates osteoblast differentiation and bone mass. Furthermore, we study how UPR dysregulation contributes to pathologic bone loss.

Role of ERAD in Bone Health: We also explore the role of ERAD in the acquisition of adult bone using murine models. Through collaboration with Dr. Ling Qi from the University of Michigan, we aim to unravel the significance of ERAD in maintaining optimal bone health.

By delving into these areas of research, the Iyer Lab aims to advance our understanding of ER homeostasis, UPR, ERAD, and their crucial roles in skeletal health and pathology.

For more information about our ongoing research projects and collaborations, please visit our lab's website or contact us directly.