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Related Concept Videos

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...
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...
Actin Polymerization and Cell Motility01:13

Actin Polymerization and Cell Motility

Actin is a family of globular proteins that are highly abundant in eukaryotic cells. It makes up approximately 1-5% of total cell protein concentration. Actin monomers polymerize to form a complex network of polarized filaments, the actin cytoskeleton, that plays a crucial role in many cellular processes, including cell motility, division, endocytosis, and metastasis of cancer cells.
Actin cytoskeleton dynamics can produce pushing, pulling, and resistance forces that help the cell to migrate.

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Related Experiment Video

Updated: Jun 22, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Kank proteins: structure, functions and diseases.

N Kakinuma1, Y Zhu, Y Wang

  • 1Signaling Molecules Research Group, Neuroscience Research Institute, National Institute of Advanced Industrial Science and Technology, AIST Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.

Cellular and Molecular Life Sciences : CMLS
|June 26, 2009
PubMed
Summary
This summary is machine-generated.

The Kank protein family (Kank1-Kank4) has a unique structure and regulates cell movement. Future studies will explore their role in cancer and developmental disorders.

Related Experiment Videos

Last Updated: Jun 22, 2026

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach
11:11

Identification of Novel CK2 Kinase Substrates Using a Versatile Biochemical Approach

Published on: February 21, 2019

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • The Kank protein family, comprising Kank1-Kank4, possesses a distinct molecular structure featuring N-terminal coiled-coil and KN motifs, alongside C-terminal ankyrin-repeats.
  • Kank1 was identified through positional cloning as a tumor suppressor gene implicated in renal cell carcinoma, with other family members discovered via homology searches.

Purpose of the Study:

  • To elucidate the structural characteristics and functional roles of the Kank protein family.
  • To investigate the involvement of Kank proteins in cellular processes such as actin polymerization and cell motility.
  • To explore the potential links between Kank proteins and various diseases, including cancer and developmental disorders.

Main Methods:

  • Positional cloning was used to identify Kank1.
  • Homology searches were employed to discover other Kank family members.
  • Analysis of signaling pathways, including PI3K/Akt, to understand Kank protein function.

Main Results:

  • Kank proteins exhibit a conserved structural organization with specific functional motifs.
  • The Kank family plays a role in regulating actin polymerization and cell motility.
  • Kank proteins are implicated in signaling pathways involving PI3K/Akt.

Conclusions:

  • The Kank protein family is structurally unique and functionally significant in regulating cellular processes.
  • Further research is warranted to fully understand the Kank family's role in cancer, neuronal, and developmental disorders.