LAMTOR1 Regulates RhoA and Kar1 in The RhoA Pathway (G55004)

Target Name: LAMTOR1

NCBI ID: G55004

LAMTOR1 Regulates RhoA and Kar1 in The RhoA Pathway

LAMTOR1 (p27Kip1-releasing factor from RhoA) is a protein that plays a crucial role in cell signaling pathways, specifically in the RhoA pathway. RhoA is a GTPase that regulates cell behavior, including cell division, migration, and cytoskeletal organization. The RhoA pathway is a complex network of proteins that work together to regulate cell signaling pathways, and LAMTOR1 is one of the key regulators in this pathway.

LAMTOR1 was first identified in the late 1990s as a protein that was expressed in a variety of tissues, including brain, heart, and muscle. The protein is composed of 250 amino acid residues and has a calculated molecular mass of 30.1 kDa. LAMTOR1 is a GTPase that uses GTPase-activating protein (GAP) and nucleotide-binding oligomerization (NBO) domains to regulate the activity of RhoA.

The RhoA pathway is a complex network of proteins that work together to regulate cell signaling pathways. The pathway is named after the protein RhoA, which is the first protein in the pathway to be discovered. RhoA is a GTPase that regulates cell behavior, including cell division, migration, and cytoskeletal organization. The RhoA pathway is a complex network of proteins that work together to regulate cell signaling pathways, and LAMTOR1 is one of the key regulators in this pathway.

LAMTOR1 is a critical regulator of the RhoA pathway. It is able to interact with RhoA and regulate its activity. LAMTOR1 is also able to interact with other proteins that are part of the RhoA pathway, including the protein Kar1 (also known as p27Kip1), which is a key regulator of the RhoA pathway. Kar1 is a GAP that is able to interact with LAMTOR1 and regulate its activity.

The RhoA pathway is involved in many cellular processes, including cell division, cell migration, and cytoskeletal organization. LAMTOR1 is a key regulator of these processes, and it is able to interact with RhoA and Kar1 to regulate the activity of these proteins.

LAMTOR1 is also involved in the regulation of other cellular processes, including cell signaling pathways and protein degradation. It is able to interact with other proteins, including the protein degradation regulator AP-1, to regulate its activity.

In conclusion, LAMTOR1 (p27Kip1-releasing factor from RhoA) is a protein that plays a crucial role in cell signaling pathways, specifically in the RhoA pathway. It is a critical regulator of this pathway and is involved in many cellular processes, including cell division, cell migration, and cytoskeletal organization. The RhoA pathway is a complex network of proteins that work together to regulate cell signaling pathways, and LAMTOR1 is one of the key regulators in this pathway. Further research into LAMTOR1 and its role in the RhoA pathway may reveal new therapeutic opportunities for the treatment of various diseases.

Protein Name: Late Endosomal/lysosomal Adaptor, MAPK And MTOR Activator 1

Functions: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to membranes. Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes. May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes. May also play a role in RHOA activation. Involved in the control of embryonic stem cells differentiation; together with FLCN it is necessary to recruit and activate RRAGC/RagC and RRAGD/RagD at the lysosomes, and to induce exit of embryonic stem cells from pluripotency via non-canonical, mTOR-independent TFE3 inactivation (By similarity)

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