Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.
Tubulin Folding Cofactor E-Like (TBCEL) is a protein that plays a crucial role in the proper folding and stability of tubulin, a key component of the microtubule cytoskeleton. Microtubules are essential for various cellular functions, including cell division, intracellular transport, and maintenance of cell shape. TBCEL is a human recombinant protein that has been studied for its involvement in tubulin dynamics and its potential implications in various diseases.
Microtubules are dynamic structures composed of α- and β-tubulin heterodimers. They undergo continuous phases of growth and shrinkage, a phenomenon known as dynamic instability. This dynamic behavior is regulated by various proteins, including tubulin-specific chaperones and microtubule-associated proteins (MAPs). Tubulin-specific chaperones, such as cofactors A to E, are responsible for the correct folding and assembly of tubulin dimers .
TBCEL is a member of the tubulin-specific chaperone family and is closely related to Tubulin Folding Cofactor E (TBCE). It is involved in the post-chaperonin tubulin folding pathway and plays a role in the assembly and stability of the tubulin complex . TBCEL acts as a regulator of tubulin stability by binding to α-tubulin and promoting its degradation through the proteasomal pathway . This function is crucial for maintaining the balance between tubulin polymerization and depolymerization, which is essential for proper microtubule dynamics.
TBCEL exerts its function by interacting with tubulin folding intermediates produced via the cytosolic chaperonin CCT (chaperonin containing TCP-1) complex. Upon overexpression, TBCEL depolymerizes microtubules by committing tubulin to proteasomal degradation . This process involves the disruption of the tubulin heterodimer, leading to an increase in the number of stable microtubules and a tight clustering of endocellular membranes around the microtubule-organizing center .
The regulation of tubulin stability by TBCEL is vital for various cellular processes. Microtubules are involved in the formation of the mitotic spindle during cell division, and their dynamic instability is crucial for accurate chromosome segregation. Additionally, microtubules play a role in intracellular transport, cell motility, and maintenance of cell polarity. Dysregulation of tubulin dynamics can lead to various diseases, including cancer and neurodegenerative disorders .
Mutations or alterations in the expression of TBCEL have been associated with certain diseases. For example, TBCEL has been linked to nonsyndromic congenital nail disorders . Understanding the role of TBCEL in tubulin dynamics and its implications in disease can provide insights into potential therapeutic targets for conditions involving microtubule dysfunction.