# VACUOLAR TARGETING RECEPTOR--STRUCTURE AND FUNCTION

> **NIH NIH R01** · UNIVERSITY OF MISSOURI-COLUMBIA · 1994 · $245,594

## Abstract

The vacuoles of yeast and plant cells share many structural and functional
features. In both, specific targeting determinants must be present on
soluble proteins for them to be sorted from the bulk secretory flow to the
vacuole. Neither the precise nature of these determinants nor the identity
of receptor(s) responsible for sorting are known for yeast or plants. We
have biochemically purified an approximate 80 kD protein from peas with
the features expected of such a receptor: (1) It is present in clathrin-
coated vesicles that are known to participate in transport of proteins
from the Golgi to the vacuole. (2) It binds with high affinity to a
peptide that is known to contain sequences necessary and sufficient to
target a cysteine protease to the vacuole, and with decreased affinity to
peptides that are less efficient in directing such targeting. (3) It is a
transmembrane protein having the peptide binding domain within its
intralumenal amino terminal portion and approximately 4 kD of the carboxyl
terminus exposed on the cytoplasmic surface.

Identification of this protein is a novel finding and may be expected to
lead to new insights into mechanisms for vacuolar sorting in both yeast
and plant cells. As yeast continue to be the major genetic system for
identifying gene products that participate in compartmentalization and
sorting of proteins in the eukaryotic secretory pathway characterization
of such a receptor is likely to lead to information that will be important
for mammalian cell biologists. Only one receptor responsible for directing
proteins to destinations from the intracellular trafficking pathway (as
distinguished from plasma membrane receptors mediating endocytosis) has
been characterized, the mannose-6-phosphate receptor. Studies of the VTR
are therefore likely to provide additional insights into mechanisms
involved in such trafficking.

Work proposed here will determine the structure, function, and biological
significance of this candidate Vacuolar Targeting Receptor (VTR). We will
use the purified protein to establish the structural requirements for
binding to different peptides, and will correlate these results with the
ability of the same peptide sequences to direct vacuolar sorting in vivo.
Antibodies to the VTR will allow its intracellular distribution and
trafficking to be characterized. A cDNA clone of the VTR will provide its
primary structure and will allow experiments to knock out expression of
VTR protein in plant cells, thereby establishing its function.

## Key facts

- **NIH application ID:** 2191446
- **Project number:** 1R01GM052427-01
- **Recipient organization:** UNIVERSITY OF MISSOURI-COLUMBIA
- **SAM.gov UEI:** SZPJL5ZRCLF4
- **Principal Investigator:** JOHN C ROGERS
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1994
- **Award amount:** $245,594
- **Award type:** 1
- **Project period:** 1994-07-01 → 1998-06-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/2191446

## Citation

> US National Institutes of Health, RePORTER application 2191446, VACUOLAR TARGETING RECEPTOR--STRUCTURE AND FUNCTION (1R01GM052427-01). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/2191446. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*