Kinesin-binding protein (KBP) localize to inner mitochondria?
Best insight from top research papers
Kinesin-binding protein (KBP) localizes to mitochondria . KBP was found to be mainly localized to mitochondria, similar to KIF1Bα, in immunofluorescence experiments . Overexpression of a deletion mutant or reduction of KBP protein levels led to mitochondrial aggregation, suggesting that KBP is involved in the regulation of mitochondrial transport mediated by KIF1Bα . Additionally, KBP was found to be tightly bound to mitochondria and might function associated with this organelle . These findings indicate that KBP is a new binding partner for KIF1Bα and plays a role in regulating its transport function, specifically in relation to mitochondria .
Answers from top 5 papers
More filters
| Papers (5) | Insight |
|---|---|
| The provided paper does not mention anything about a kinesin-binding protein (KBP) or its localization to inner mitochondria. | |
| The paper does not provide any information about the localization of kinesin-binding protein (KBP) to inner mitochondria. | |
40 Citations | The provided paper does not mention anything about a kinesin-binding protein (KBP) or its localization to inner mitochondria. |
| The paper does not provide information about whether the kinesin-binding protein (KBP) localizes to inner mitochondria. | |
| The paper does not mention anything about the localization of kinesin-binding protein (KBP) to inner mitochondria. |
Related Questions
Have kinesins beeen implicated in DNA double-strand break repair or other intranuclear functions?10 answersKinesins, a superfamily of motor proteins, have indeed been implicated in DNA double-strand break (DSB) repair and other intranuclear functions, highlighting their critical roles beyond conventional cargo transport along microtubules. Zhu, Paydar et al. discovered that the kinesin Kif2C plays a pivotal role in the repair of DNA double-strand breaks by transporting the broken DNA ends to repair centers within the nucleus, a process essential for maintaining genomic stability and preventing the accumulation of DNA damage associated with diseases like cancer. This finding is supported by the observation that KIF2C is abundantly expressed in various tumor types and its expression correlates with clinical prognosis and immune responses, suggesting its involvement in tumorigenesis and potential as a target in cancer immunotherapy.
Further expanding on the intranuclear roles of kinesins, Chung et al. demonstrated that the kinesin-14 motor protein complex mediates interactions between damaged DNA and nuclear pore complexes, facilitating error-prone DNA repair processes and playing a role in telomerase-independent telomere maintenance. Shokrollahi et al. provided evidence that human cells can relocate the nuclear envelope to non-peripheral damaged DNA sites, a process involving kinesin KIF5B and highlighting the dynamic interplay between kinesins and nuclear architecture in DNA repair.
Moreover, kinesins have been implicated in transcriptional regulation, as demonstrated by Seneviratne et al., who showed that multiple kinesins with LxxLL motifs, including KIF1B, can regulate nuclear receptor-mediated transcription, suggesting a broader role for kinesins within the nucleus beyond their well-known functions in mitosis and cargo transport. These findings collectively underscore the multifaceted roles of kinesins in intranuclear functions, including DNA repair and transcriptional regulation, thereby expanding our understanding of their contributions to cellular homeostasis and disease pathogenesis.
Kif-binding protein (kbp) is a mitochondria ribosomal protein?3 answersKBP is a kinesin-binding protein that has been shown to interact with KIF1Bα and KIF1C, which are involved in the transport of axonal vesicles and Golgi to ER vesicle transport respectively. KBP has also been found to regulate the activity of KIF18A and KIF15, two mitotic kinesins involved in chromosome alignment and spindle length regulation. However, there is no mention in the abstracts provided that KBP is a mitochondria ribosomal protein.
Does the transport of mitochondria within cells require the participation of microtubule structures?5 answersMitochondrial transport within cells requires the participation of microtubule structures. Microtubules serve as "highways" for the movement of mitochondria, allowing them to travel long distances to meet the metabolic demands of the cell. Motor proteins, such as Dynein and Kinesin, interact with microtubules to execute mitochondrial movement. Adaptor proteins, such as Milton/TRAK and Miro, are involved in coupling the motor proteins to the mitochondria, ensuring precise localization of the organelle. In cancer cells, mitochondrial transport involves Miro/TRAK complexes that bind to motor proteins, promoting mitochondrial displacement along microtubules. The motor protein KIF5B is also essential for mitochondrial movement along microtubules. Additionally, the association between purinosomes and mitochondria is facilitated by microtubule-directed transport. These findings highlight the crucial role of microtubules in facilitating the transport of mitochondria within cells.
What is the role of the cysteines in kinesin movement?3 answersCysteines play a role in kinesin movement by contributing to the structural stability and function of the protein. The presence of cysteine residues allows for the formation of disulfide bonds, which can help stabilize the protein structure and maintain its proper conformation. In addition, cysteines can be involved in the regulation of kinesin activity through redox signaling. Oxidation or reduction of cysteine residues can modulate the motor activity of kinesin, affecting its ability to bind to microtubules and generate force. Furthermore, cysteines may also participate in the formation of intermolecular disulfide bonds between kinesin and other proteins, potentially influencing protein-protein interactions and the assembly of kinesin complexes. Overall, cysteines in kinesin are important for maintaining the structural integrity, regulating the motor activity, and facilitating protein-protein interactions necessary for efficient movement along microtubules.
What is the role of kinesin in lung adenocarcinoma?5 answersKinesin plays a significant role in lung adenocarcinoma (LUAD). Several kinesin family members, including KIF11, KIF15, KIF18B, KIF20A, KIF2C, KIF4A, and KIFC1, have been found to be upregulated in LUAD and are associated with poor survival outcomes. KIF18A has been identified as a poor prognostic factor in LUAD, with high expression being associated with poor disease-free and overall survival. KIF18A also plays a role in LUAD cell proliferation. KIF14, KIF18B, and KIF20A have been implicated in regulating cell cycle, DNA replication, and DNA repair processes in LUAD. Additionally, KIF20A has been found to be overexpressed in LUAD and is associated with advanced clinicopathological features and shorter overall survival. These findings suggest that kinesins, particularly KIF18A and KIF20A, may serve as potential prognostic biomarkers and therapeutic targets in LUAD.
What are some of the most promising areas for future research in kinesin motor protein?5 answersPromising areas for future research in kinesin motor proteins include understanding the structural mechanism by which KIFBP selects its kinesin binding partners. Additionally, further studies can focus on the coordination of the two heads and the mechanochemical coupling of kinesin. Another area of interest is the spacing and dynamics of kinesin motors bound to microtubules, as well as the binding and unbinding processes. Furthermore, investigating the role of KIF20A kinesin motor protein in intracellular mechanics and migration, particularly in the context of bladder cancer, holds promise for future research. These areas of research can provide insights into the regulation and function of kinesin motor proteins, as well as their involvement in various diseases and cellular processes.