Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Plasmodesmata02:32

Plasmodesmata

32.8K
The organs in a multicellular organism’s body are made up of tissues formed by cells. To work together cohesively, cells must communicate. One way that cells communicate is through direct contact with other cells. The points of contact that connect adjacent cells are called intercellular junctions.
32.8K
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

2.1K
Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
2.1K
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

2.0K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
2.0K
Cell Adhesion in Plants01:14

Cell Adhesion in Plants

2.7K
Plants have rigid cell walls that are made up of cell wall polysaccharides that mediate cell-cell adhesion. The primary cell walls of plants consist of two independent and interacting polysaccharide networks: a pectin matrix that embeds the second network comprising cellulose and hemicelluloses.
Pectins are complex heteropolymers mainly composed of negatively-charged α-D-glucopyranosyl uronic acid and some neutral glycosyl residues such as α-L-rhamnopyranose, α-L-arabinofuranose,...
2.7K
Cell Signaling in Plants01:25

Cell Signaling in Plants

5.7K
Plant cells communicate to coordinate their cycle of growth, flowering and fruiting, and activities in roots, shoots, and leaves in response to the changing environmental conditions. Plant signaling is distinct from animal signaling. Plants primarily utilize enzyme-linked receptors, whereas the largest class of cell-surface receptors in animals are G-protein coupled receptors (GPCRs). Unlike animals, receptor tyrosine kinases are rare in plants. Instead, plants have a diverse class of...
5.7K
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

2.3K
Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
2.3K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

In situ architecture of plasmodesmata in Physcomitrium patens resolved by cryo-electron tomography.

Nature plants·2026
Same author

A Novel Phloem-Specific HVA22-Like Protein Facilitates Protein Movement via Plasmodesmata in Potato.

Contact (Thousand Oaks (Ventura County, Calif.))·2026
Same author

Should I stay or should I go-does protein localization to plasmodesmata depend on targeting signals?

Journal of experimental botany·2025
Same author

Root-derived cytokinin regulates Arabidopsis flowering time through components of the age pathway.

Plant physiology·2025
Same author

Live-cell RNA imaging with the inactivated endonuclease Csy4 enables new insights into plant virus transport through plasmodesmata.

PLoS pathogens·2025
Same author

Tomato SlGSTU38 interacts with the PepMV coat protein and promotes viral infection.

The New phytologist·2023

Related Experiment Video

Updated: Jul 18, 2025

Identification of Plasmodesmal Localization Sequences in Proteins In Planta
08:07

Identification of Plasmodesmal Localization Sequences in Proteins In Planta

Published on: August 15, 2017

8.3K

Heavy Metal-Associated Isoprenylated Plant Proteins (HIPPs) at Plasmodesmata: Exploring the Link between Localization

Zoe Kathleen Barr1,2, Tomáš Werner3, Jens Tilsner1,2

  • 1Biomedical Sciences Research Complex, University of St Andrews, BMS Building, North Haugh, St Andrews, Fife KY16 9ST, UK.

Plants (Basel, Switzerland)
|August 26, 2023
PubMed
Summary

Heavy metal-associated isoprenylated plant proteins (HIPPs) are unique plant proteins. This review explores HIPPs in plasmodesmata (PD) and their potential roles in plant cell communication and stress responses.

Keywords:
HIPPabiotic and biotic stresscytokininheavy metal-associated plant proteinsmetallochaperoneplasmodesmataprenylation

More Related Videos

Author Spotlight: Microscopic Analysis of Protein Localization at Plasmodesmata in Plants
05:54

Author Spotlight: Microscopic Analysis of Protein Localization at Plasmodesmata in Plants

Published on: November 1, 2024

2.2K
Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

8.4K

Related Experiment Videos

Last Updated: Jul 18, 2025

Identification of Plasmodesmal Localization Sequences in Proteins In Planta
08:07

Identification of Plasmodesmal Localization Sequences in Proteins In Planta

Published on: August 15, 2017

8.3K
Author Spotlight: Microscopic Analysis of Protein Localization at Plasmodesmata in Plants
05:54

Author Spotlight: Microscopic Analysis of Protein Localization at Plasmodesmata in Plants

Published on: November 1, 2024

2.2K
Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins
11:11

Determination of Plasma Membrane Partitioning for Peripherally-associated Proteins

Published on: June 15, 2018

8.4K

Area of Science:

  • Plant Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Heavy metal-associated isoprenylated plant proteins (HIPPs) are a unique protein family in vascular plants.
  • HIPPs feature heavy metal-binding domains and isoprenylation sites, enabling posttranslational lipid modification.
  • HIPPs have diverse functionalities, with many identified in plasmodesmata (PD) proteomes.

Purpose of the Study:

  • To review the known functions of PD-localized HIPPs.
  • To explore how HIPP structure and function relate to PD properties and regulation.
  • To highlight HIPPs as potential regulators of intercellular communication and stress responses.

Main Methods:

  • Literature review of existing studies on HIPPs and plasmodesmata.
  • Analysis of HIPP structural features and known functional roles.
  • Integration of knowledge on HIPPs with PD biology.

Main Results:

  • HIPPs are found in PD, which are crucial for symplastic connectivity and intercellular communication.
  • Many HIPPs are involved in stress responses, suggesting a role in PD-mediated signaling.
  • The unique structure of HIPPs may facilitate their function in PD regulation.

Conclusions:

  • PD-localized HIPPs are promising candidates for regulating intercellular communication and stress responses.
  • Further research into HIPP structure-function relationships in PD is warranted.
  • HIPPs represent a key link between cellular stress, signaling, and plant development via PD.