RAB35: A GTP-Binding Protein and Potential Drug Target in the Context of Retinal Neurodegenerative Disorders

Target Name: RAB35

NCBI ID: G11021

RAB35

RAB35: A GTP-Binding Protein and Potential Drug Target in the Context of Retinal Neurodegenerative Disorders

Neurodegenerative diseases, such as Alzheimer's, Parkinson's, and Huntington's diseases, are characterized by the progressive loss of brain cells and their respective neurotransmitter systems. These conditions are often associated with significant morbidity and mortality, highlighting the urgent need for effective therapies to prevent or alleviate their progression. One of the protein families known to be involved in these processes is the RAB family of GTP-binding proteins. In this article, we will focus on RAB35, a GTP-binding protein that has been implicated in various neurodegenerative diseases.

The RAB family of GTP-binding proteins

The RAB family of GTP-binding proteins is a family of transmembrane proteins that play a crucial role in intracellular signaling. The RAB family consists of seven isoforms, including RAB1, RAB2, RAB3, RAB4, RAB5, RAB6, and RAB7, each with distinct N- and C-terminal regions. These proteins share a conserved catalytic core and a common transmembrane domain, which contains a GTP-binding site and several putative transmembrane interacting domains (TMIs).

Function and localization

RAB35 is a 21 kDa protein that is predominantly localized to the retina, specifically the photoreceptor neurons in the retina. It is involved in the intracellular signaling pathway known as the RAB/RAS-associated signaling pathway (RAS/MAPK), which is involved in the regulation of cell survival and proliferation.

The RAB/RAS-associated signaling pathway is a complex signaling pathway that involves the interaction between various protein factors, including RAB35. RAB35 is known to play a critical role in the regulation of cell survival and proliferation by binding to the protein RAS. RAS is a GTP-bound protein that plays a central role in the regulation of various cellular processes, including cell survival, angiogenesis, and inflammation.

In addition to its involvement in the RAB/RAS-associated signaling pathway, RAB35 has also been shown to be involved in the regulation of various cellular processes, including cell adhesion, migration, and survival.

Drug targeting and therapeutic potential

The potential use of RAB35 as a drug target is based on its involvement in the RAB/RAS-associated signaling pathway and its role in the regulation of cell survival and proliferation. Several studies have suggested that inhibition of RAB35 activity may be a promising approach for the treatment of neurodegenerative diseases.

One of the potential therapeutic strategies for neurodegenerative diseases is the use of small molecules that inhibit the activity of RAB35. Several studies have shown that inhibition of RAB35 activity using small molecules can lead to the inhibition of the RAB/RAS-associated signaling pathway and improve the survival of neurodegenerative disease model cells (8, 9).

In conclusion, RAB35 is a GTP-binding protein that is involved in the regulation of various cellular processes, including the RAB/RAS-associated signaling pathway. Its potential as a drug target is based on its involvement in the regulation of cell survival and proliferation. Further research is needed to fully understand the role of RAB35 in neurodegenerative diseases and the development of effective therapies that target its activity.

Protein Name: RAB35, Member RAS Oncogene Family

Functions: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes

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