Dynamic testicular adhesion junctions are immunologically unique. I. Localization of p120 catenin in rat testis

Kamin J Johnson1, Kim Boekelheide

  • 1Department of Pathology and Laboratory Medicine, Brown University, 175 Meeting Street, Providence, Rhode Island 02912, USA. kamin_johnson@brown.edu

Insights

p120 catenin is a key component of desmosome-like junctions in the rat testis, with specific isoforms localizing to distinct cell junctions. This study reveals unique molecular compositions in Sertoli-germ cell junctions, crucial for understanding testis development and function.

Area of Science:

  • Reproductive Biology
  • Cell Biology
  • Molecular Biology

Background:

  • The seminiferous epithelium relies on diverse junctions for cell adhesion.
  • The molecular composition of Sertoli-Sertoli and Sertoli-germ cell junctions is not fully understood.
  • Catenins are critical for regulating adhesion strength at adherens junctions.

Purpose of the Study:

  • To investigate the localization and role of p120 catenin (p120) in rat testis junctions.
  • To determine the molecular composition of inter-Sertoli and Sertoli-germ cell junctions.
  • To identify specific p120 isoforms associated with different junction types.

Main Methods:

  • Immunofluorescence using monoclonal antibodies (5A7, 8D11, 15D2) on rat testis cryosections and touch preparations.
  • Immunoprecipitation of testis homogenates to identify p120 isoforms.
  • Colocalization studies with beta-catenin and plectin.

Main Results:

  • At least four p120 catenin isoforms are expressed from postnatal day 7 through adulthood.
  • p120 catenin is present in both inter-Sertoli and Sertoli-germ cell junctions.
  • Antibodies 5A7 and 8D11 colocalize with beta-catenin and plectin at inter-Sertoli and Sertoli-spermatocyte junctions, suggesting p120 is part of desmosome-like junctions.
  • Antibody 15D2 specifically labels Sertoli-round spermatid and newly formed inter-Sertoli junctions in a dynamic, stage-specific pattern.

Conclusions:

  • p120 catenin is a component of most desmosome-like junctions in the rat testis.
  • Different cell types exhibit unique molecular compositions within their desmosome-like junctions.
  • The dynamic localization of p120 suggests its involvement in the remodeling of these junctions during spermatid differentiation.

Related Concept Videos

Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
Catenins bind to cell adhesion molecules such as cadherins and link them to different cytoskeletal proteins depending on the type of cell junction. At the adherens...
Adherens Junctions01:24

Adherens Junctions

Strong contact points between adjacent cells anchor them to each other, forming tissues. Such anchoring junctions are of two types –  adherens junctions and desmosomes. Adherens junctions are abundant in tissues such as  epithelium and endothelium, forming a continuous zone of adhesion called the adhesion belt. In other tissues, such as  heart muscle, they appear as clusters, linking the cells to produce coordinated heart muscle contraction.
Adherens Junctions are Dynamic
The endothelial cells...
Tight Junctions01:29

Tight Junctions

Tight junctions are molecular seals between cells that prevent the leaking of fluids, ions, and other small solutes across cavities and compartments in multicellular organisms. They are mainly composed of claudin and occludin transmembrane proteins, and other proteins such as tricellulin and JAM (junctional adhesion molecule). All these proteins are 4-pass transmembrane proteins, except JAM, which is a single-pass transmembrane protein belonging to the immunoglobulin superfamily. The...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Tension Response at Adherens Junctions01:26

Tension Response at Adherens Junctions

The adherens junctions that anchor cells together are multi-protein complexes that dynamically adapt to mechanical stimuli such as tensile forces and shear stress. Mechanosensory proteins in these junctions can sense such mechanical stimuli and undergo a shift in their conformation, resulting in an altered function — a process called mechanotransduction.
α-Catenin as a Mechanosensory Protein
The α-catenin of adherens junctions is an allosteric protein with three VH (vinculin homology) domains...