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

Laminins are the Adhesive Proteins of Basal Lamina00:55

Laminins are the Adhesive Proteins of Basal Lamina

Laminins are heterotrimeric proteins with high molecular mass found in the extracellular matrix. Each laminin molecule is composed of three chains, viz. alpha, beta, and gamma, coded by five, four, and three paralogous genes, respectively. Laminins are categories based on the compositions of the three chains.
In humans, the five forms of alpha chains are LAMA 1, LAMA 2, LAMA 3, LAMA 4, and LAMA 5. The four forms of beta chains are LAMB 1, LAMB 2, LAMB 3, and LAMB 4. The three forms of gamma...
Cytoskeletal Linker Proteins - Plakins01:09

Cytoskeletal Linker Proteins - Plakins

Plakins are large proteins with binding domains for microtubules, microfilaments, intermediate filaments, and membrane-associated protein complexes at cell junctions. Plakin functions are evolutionarily conserved and are primarily involved in organizing the different components of the cytoskeleton by crosslinking them to each other and connecting them to the cell-matrix and cell adhesion complexes. They are also known to interact with signal transducers, serve as scaffolds for signaling...
Basal Lamina are the Specialized Form of ECM01:03

Basal Lamina are the Specialized Form of ECM

The basal lamina is a thin extracellular layer that lies underneath the cells and separates them from other tissues. The three layers of the basal lamina are lamina lucida, lamina densa and lamina reticularis. The basal lamina, a mixture of glycoproteins and collagen, provides an attachment site for the epithelium, separating it from underlying connective tissue. The framework of basal lamina has other essential proteins such as laminins mesh, perlecan, entactin, and type IV collagen.
Proteins...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Formation of Lipopolysaccharides01:19

Formation of Lipopolysaccharides

Lipopolysaccharides (LPS) are crucial components of the outer membrane of Gram-negative bacteria, serving both structural and functional roles. It contributes to membrane stability and protects bacteria from host immune responses. LPS is composed of three major regions—lipid A, a core oligosaccharide, and an O antigen. The biosynthesis and assembly of LPS involve a highly coordinated set of enzymatic reactions and transport mechanisms. Additionally, LPS is recognized as an endotoxin, triggering...

You might also read

Related Articles

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

Sort by
Same author

LAP2α drives breast tumorigenesis by mitigating replication stress.

Cell death & disease·2026
Same author

The unfolded protein response in progeria arteries originates from non-endothelial cell types.

Life science alliance·2025
Same author

Emerin is an effector of oncogenic KRAS-driven nuclear dynamics in pancreatic cancer.

JCI insight·2025
Same author

MyoD1 localization at the nuclear periphery is mediated by association of WFS1 with active enhancers.

Nature communications·2025
Same author

Lamin chromatin binding is modulated by interactions of different LAP2α domains with lamins and chromatin.

iScience·2024
Same author

LAP2alpha facilitates myogenic gene expression by preventing nucleoplasmic lamin A/C from spreading to active chromatin regions.

Nucleic acids research·2024
Same journal

Evolutionary and Biochemical Perspectives on the Incorporation and Utilization of Selenocysteine.

Cold Spring Harbor perspectives in biology·2026
Same journal

The Mitochondrial Calcium Uniporter: From Parts to Signaling Networks.

Cold Spring Harbor perspectives in biology·2026
Same journal

Growth Control and Beyond: Functional Diversity and Regulation of the Hippo Pathway in the Nervous System.

Cold Spring Harbor perspectives in biology·2026
Same journal

Structural Studies of Core Hippo Pathway Components.

Cold Spring Harbor perspectives in biology·2026
Same journal

The Hippo Pathway in Intestinal Regeneration, Fetal Reprogramming, and Tumorigenesis.

Cold Spring Harbor perspectives in biology·2026
Same journal

A Synergy between Genetics and Biochemistry Unravels the Molecular Architecture of the Hippo Signaling Pathway.

Cold Spring Harbor perspectives in biology·2026
See all related articles

Related Experiment Video

Updated: Jun 13, 2026

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

Lamin-binding Proteins.

Katherine L Wilson1, Roland Foisner

  • 1Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.

Cold Spring Harbor Perspectives in Biology
|May 11, 2010
PubMed
Summary
This summary is machine-generated.

Nuclear lamins (A- and B-type) interact with numerous proteins to maintain nuclear structure and regulate gene expression. These interactions are crucial for nuclear architecture, chromatin organization, and cellular processes.

More Related Videos

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies

Published on: March 19, 2014

Related Experiment Videos

Last Updated: Jun 13, 2026

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence
06:23

Detection of Nuclear Blebbing and DNA Leakage in Mammalian Cells by Immunofluorescence

Published on: January 17, 2025

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells
06:56

Generating a Fractal Microstructure of Laminin-111 to Signal to Cells

Published on: September 28, 2020

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies
13:52

Efficient Production and Purification of Recombinant Murine Kindlin-3 from Insect Cells for Biophysical Studies

Published on: March 19, 2014

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • A- and B-type lamins form the nuclear lamina, a key structural component of the nucleus.
  • Lamins interact with various proteins, influencing nuclear architecture and function.
  • These interactions occur at the inner nuclear membrane and within the nucleus.

Purpose of the Study:

  • To explore the diverse functions of lamin-binding proteins.
  • To understand how lamins and their binding partners contribute to nuclear organization and gene regulation.
  • To elucidate the role of transient lamin interactions in nuclear processes.

Main Methods:

  • The study is a review of existing literature.
  • It synthesizes findings on protein-protein interactions involving lamins.
  • Focuses on the functional consequences of these interactions.

Main Results:

  • Lamin-binding proteins anchor lamins to the nuclear envelope, maintaining nuclear integrity.
  • Inner membrane proteins link the nuclear lamina to the cytoskeleton.
  • Lamin-binding proteins act as adaptors organizing chromatin, regulating gene expression, and modulating signaling pathways.
  • Transient lamin interactions support transcription and replication machinery.

Conclusions:

  • Lamin-binding proteins are essential for nuclear architecture, chromatin organization, and gene regulation.
  • The nuclear lamina network, through its interactions, plays a critical role in fundamental cellular processes.
  • Further research into these interactions can reveal insights into nuclear function and disease.