# Molecular mechanisms of membrane protein homeostasis at the Golgi

> **NIH NIH R35** · CORNELL UNIVERSITY · 2024 · $45,792

## Abstract

Project summary/Abstract
 The Golgi complex plays a prominent role in secretory and endocytic trafficking in eukaryotic cells
and is key to the biosynthesis of glycoconjugates (glycoproteins and glycolipids) that are essential for
life. Golgi resident proteins, such as glycosyltransferases and sugar nucleotide transporters, are precisely
distributed across the Golgi stacks by recycling mechanisms that counteract the flow of ongoing vesicular
transport. Dysfunction in these mechanisms, or their hijacking by viruses and toxins, is known to have
serious consequences for human health, leading to congenital disorders of glycosylation, cancers, and
immune dysfunction.
 Membrane proteins residing in various Golgi compartments are well annotated; however, the mecha-
nistic basis of how most Golgi proteins are selected for recycling, or how these processes are regulated
are poorly understood. My lab is interested in uncovering these fundamental mechanisms governing
Golgi homeostasis using a multifaceted approach combining genetics, flow-cytometry, imaging, in vitro
reconstitution, and proteomics. In preliminary results, we have identified novel transmembrane compo-
nents orchestrating recycling of specific subsets of Golgi enzymes. Our findings have opened doors for
interrogating new players and dissecting the mechanisms critical to maintain Golgi identity and function.
Over the next five years, our goals are to (1) identify novel recycling receptors required at different Golgi
compartments and establish a systematic map of the intra-Golgi recycling network, (2) determine how
the transmembrane receptors engage with their cargos, and (3) define the novel functions of a disease-
associated membrane transporter in solute transport and protein recycling in the Golgi. The combined
results of our experiments will elucidate how multiple recycling pathways sustain normal Golgi function,
and how this homeostasis is disrupted in human disease.

## Key facts

- **NIH application ID:** 10915860
- **Project number:** 3R35GM150863-01S1
- **Recipient organization:** CORNELL UNIVERSITY
- **Principal Investigator:** Richa Sardana
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $45,792
- **Award type:** 3
- **Project period:** 2023-07-01 → 2028-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10915860

## Citation

> US National Institutes of Health, RePORTER application 10915860, Molecular mechanisms of membrane protein homeostasis at the Golgi (3R35GM150863-01S1). Retrieved via AI Analytics 2026-05-26 from https://api.ai-analytics.org/grant/nih/10915860. Licensed CC0.

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