ARL1
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Official Full Name
ADP-ribosylation factor-like 1
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Overview
The protein encoded by this gene belongs to the ARL (ADP-ribosylation factor-like) family of proteins, which are structurally related to ADP-ribosylation factors (ARFs). ARFs, described as activators of cholera toxin (CT) ADP-ribosyltransferase activity, regulate intracellular vesicular membrane trafficking, and stimulate a phospholipase D (PLD) isoform. Although, ARL proteins were initially thought not to activate CT or PLD, later work showed that they are weak stimulators of PLD and CT in a phospholipid dependent manner. [provided by RefSeq, Jul 2008] -
Synonyms
ARL1; ADP-ribosylation factor-like 1; ARFL1; ADP-ribosylation factor-like protein 1;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Human
- Mouse
- Rat
- Zebrafish
- E.coli
- E.Coli or Yeast
- HEK293
- HEK293T
- Human
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- Myc
- DDK
- MYC
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
ARL1 involved in several pathways and played different roles in them. We selected most pathways ARL1 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with ARL1 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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ARL1 has several biochemical functions, for example, GTP binding, GTPase activity, enzyme activator activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ARL1 itself. We selected most functions ARL1 had, and list some proteins which have the same functions with ARL1. You can find most of the proteins on our site.
Function | Related Protein |
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GTP binding | RAB5B;RHOB;ARL3L1;IRGQ;EEF2A.2;TUBA3D;AGAP1;RND1;RHOUA |
GTPase activity | DNAJC27;RAB27A;RAB33A;RALAA;GEM;RAP1GAP;RALBA;RAB13;RAB4B |
enzyme activator activity | PITRM1;SAE1;MGST2;CLPSL1;ASAP2;TAB1;TIMP2;DBNL;MMP24 |
metal ion binding | CHPT1;WBP4;MSS51;COQ7;GNAI2;GIT2A;CHPF;RARGB;CYP2D26 |
protein domain specific binding | ACSL3;MPP7;PKD1;VRK2;PLAUR;YWHAE1;PLG;WNT1;ARRB2 |
ARL1 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ARL1 here. Most of them are supplied by our site. Hope this information will be useful for your research of ARL1.
GCC2; RIOK3; HLA-B; CDK5RAP3; C20orf24; BRF2; GSTK1; PHLDA3; q81z98_bacan; pi3p; PTBP3; MYC; MME; NEDD1
- Q&As
- Reviews
Q&As (16)
Ask a questionYes, ARL1 can undergo post-translational modifications such as lipidation with myristate or palmitate groups. These modifications aid in membrane association and regulate the localization and function of ARL1 in vesicular trafficking.
Currently, there are no known genetic disorders directly associated with ARL1 mutations. However, dysregulation of vesicular trafficking processes, for which ARL1 is essential, can contribute to pathological conditions. Further research may uncover potential links between ARL1 dysfunction and specific genetic disorders.
While the primary role of ARL1 is in vesicular trafficking, recent studies have suggested additional functions for ARL1 in autophagy, cilia formation, and cytoskeleton organization. These emerging roles expand the potential impact of ARL1 in maintaining cellular homeostasis.
While there is no direct association between ARL1 mutations and specific diseases, dysregulation of ARL1-mediated vesicular trafficking processes can contribute to pathological conditions. For example, defects in Golgi-ER trafficking and autophagy have been linked to neurodegenerative diseases and cancer, suggesting potential roles for ARL1 dysfunction in these disorders.
ARL1 is expressed in a wide range of cell types and tissues, suggesting its ubiquitous presence in most cellular systems. However, its expression levels may vary depending on the specific cell type and the physiological state of the cell.
ARL1 itself is not extensively involved in signaling pathways. However, its interactions with effector proteins indirectly contribute to the regulation of various signaling cascades, such as the Wnt signaling pathway and the MAPK/ERK pathway, which are crucial for cell growth, development, and differentiation.
Currently, no specific human diseases have been directly linked to ARL1 dysfunction. However, alterations in vesicular trafficking processes, for which ARL1 is essential, can contribute to various pathological conditions such as neurodegenerative disorders and certain cancers.
Currently, there are no specific drugs or compounds developed to directly modulate ARL1 activity. However, as our understanding of ARL1 function advances, it may provide insights into potential targets for therapeutic intervention in diseases related to vesicular trafficking defects.
ARL1 is primarily localized to the Golgi apparatus and the ER, where it regulates vesicular trafficking events between these organelles. However, studies have also reported a partial distribution of ARL1 in other cellular compartments, including the plasma membrane and the trans-Golgi network, suggesting its involvement in diverse membrane trafficking pathways.
ARL1 shares similarities with other small GTPases, such as the ADP-ribosylation factor (ARF) proteins. While ARL1 and ARF proteins belong to the same GTPase superfamily, they have distinct functions and interactions with specific effector proteins. However, cross-talk between ARL1 and ARF proteins may occur in some cellular contexts, regulating membrane trafficking processes.
ARL1 regulates the recruitment and actions of effector proteins involved in vesicle tethering, fusion, and cargo sorting between the Golgi apparatus and ER. By facilitating these processes, ARL1 ensures efficient and accurate transport of proteins and lipids, maintaining the overall integrity and function of the endomembrane system within the cell.
Yes, ARL1 interacts with various effector proteins involved in vesicular trafficking, such as GRIP domain-containing ARF-binding protein 2 (GGA2), golgin subfamily A member 1 (GOLGA1), and golgin subfamily B member 1 (GOLGB1). These interactions facilitate the targeting and fusion of vesicles at specific cellular compartments.
Depletion or knockout of ARL1 in cells has been reported to cause disrupted Golgi-ER trafficking, altered lysosome morphology, impaired autophagy, and defects in cilia formation. These consequences highlight the critical role of ARL1 in maintaining organelle dynamics and cellular processes.
Current research on ARL1 focuses on elucidating its precise molecular mechanisms and identifying additional binding partners and effector proteins. Additionally, studies are exploring the functional implications of ARL1 in diseases with vesicular trafficking defects, which may offer new therapeutic strategies.
Currently, no specific therapeutics have been developed to directly target ARL1. However, understanding its role in vesicular trafficking may provide insights into potential therapeutic strategies for diseases associated with dysregulated vesicular transport processes.
ARL1 protein is activated by the exchange of GDP (guanosine diphosphate) for GTP (guanosine triphosphate) through the action of guanine nucleotide exchange factors (GEFs). Once activated, ARL1 interacts with effector proteins to carry out its cellular functions.
Customer Reviews (8)
Write a reviewThe ARL1 protein is renowned for its exceptional quality, making it a perfect match for my experimental requirements.
Researchers have successfully utilized ARL1 protein in electron microscopy studies, unraveling crucial insights into protein interactions and conformational changes.
This can involve organizing conferences, workshops, and webinars to discuss the latest advancements, share research findings, and broaden the understanding of ARL1 function
the ARL1 protein exhibits superior performance across a range of experimental applications.
In addition to its high-quality attributes, the manufacturer of the ARL1 protein offers exemplary technical support.
The exceptional performance of ARL1 protein in both ELISA and protein electron microscopy structure analysis positions it as a valuable tool in a broad range of research applications.
This technical support is invaluable, especially for researchers who may be new to working with ARL1 protein or if they encounter specific difficulties while conducting their experiments.
Its versatility allows for its successful implementation in diverse areas such as molecular biology, cellular assays, and protein-protein interactions.
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